data_7HUG
# 
_entry.id   7HUG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HUG         pdb_00007hug 10.2210/pdb7hug/pdb 
WWPDB D_1001407945 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HUG 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                            15892.732 1  3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-N~1~-(3-methylphenyl)piperidine-1,3-dicarboxamide' 261.320   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                               65.409    1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                     78.133    2  ?         ? ? ? 
5 water       nat water                                                    18.015    78 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-N~1~-(3-methylphenyl)piperidine-1,3-dicarboxamide' A1BRE 
3 'ZINC ION'                                               ZN    
4 'DIMETHYL SULFOXIDE'                                     DMS   
5 water                                                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BRE non-polymer         . '(3S)-N~1~-(3-methylphenyl)piperidine-1,3-dicarboxamide' ? 'C14 H19 N3 O2'  261.320 
ALA   'L-peptide linking' y ALANINE                                                  ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                 ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                               ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                          ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                 ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                     ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                          ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                  ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                    ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                               ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                  ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                   ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                               ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                            ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                  ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                   ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                               ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                 ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                   ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                               ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BRE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BRE 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1BRE 1  201 201 A1BRE LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 6   DMS   DMS A . 
E 4 DMS   1  204 7   DMS   DMS A . 
F 5 HOH   1  301 81  HOH   HOH A . 
F 5 HOH   2  302 24  HOH   HOH A . 
F 5 HOH   3  303 15  HOH   HOH A . 
F 5 HOH   4  304 56  HOH   HOH A . 
F 5 HOH   5  305 59  HOH   HOH A . 
F 5 HOH   6  306 38  HOH   HOH A . 
F 5 HOH   7  307 43  HOH   HOH A . 
F 5 HOH   8  308 9   HOH   HOH A . 
F 5 HOH   9  309 72  HOH   HOH A . 
F 5 HOH   10 310 25  HOH   HOH A . 
F 5 HOH   11 311 1   HOH   HOH A . 
F 5 HOH   12 312 11  HOH   HOH A . 
F 5 HOH   13 313 65  HOH   HOH A . 
F 5 HOH   14 314 83  HOH   HOH A . 
F 5 HOH   15 315 37  HOH   HOH A . 
F 5 HOH   16 316 68  HOH   HOH A . 
F 5 HOH   17 317 3   HOH   HOH A . 
F 5 HOH   18 318 28  HOH   HOH A . 
F 5 HOH   19 319 26  HOH   HOH A . 
F 5 HOH   20 320 44  HOH   HOH A . 
F 5 HOH   21 321 10  HOH   HOH A . 
F 5 HOH   22 322 27  HOH   HOH A . 
F 5 HOH   23 323 66  HOH   HOH A . 
F 5 HOH   24 324 4   HOH   HOH A . 
F 5 HOH   25 325 12  HOH   HOH A . 
F 5 HOH   26 326 16  HOH   HOH A . 
F 5 HOH   27 327 31  HOH   HOH A . 
F 5 HOH   28 328 18  HOH   HOH A . 
F 5 HOH   29 329 13  HOH   HOH A . 
F 5 HOH   30 330 55  HOH   HOH A . 
F 5 HOH   31 331 5   HOH   HOH A . 
F 5 HOH   32 332 42  HOH   HOH A . 
F 5 HOH   33 333 41  HOH   HOH A . 
F 5 HOH   34 334 73  HOH   HOH A . 
F 5 HOH   35 335 17  HOH   HOH A . 
F 5 HOH   36 336 53  HOH   HOH A . 
F 5 HOH   37 337 45  HOH   HOH A . 
F 5 HOH   38 338 22  HOH   HOH A . 
F 5 HOH   39 339 40  HOH   HOH A . 
F 5 HOH   40 340 75  HOH   HOH A . 
F 5 HOH   41 341 57  HOH   HOH A . 
F 5 HOH   42 342 61  HOH   HOH A . 
F 5 HOH   43 343 29  HOH   HOH A . 
F 5 HOH   44 344 70  HOH   HOH A . 
F 5 HOH   45 345 8   HOH   HOH A . 
F 5 HOH   46 346 60  HOH   HOH A . 
F 5 HOH   47 347 76  HOH   HOH A . 
F 5 HOH   48 348 58  HOH   HOH A . 
F 5 HOH   49 349 32  HOH   HOH A . 
F 5 HOH   50 350 14  HOH   HOH A . 
F 5 HOH   51 351 6   HOH   HOH A . 
F 5 HOH   52 352 79  HOH   HOH A . 
F 5 HOH   53 353 19  HOH   HOH A . 
F 5 HOH   54 354 52  HOH   HOH A . 
F 5 HOH   55 355 33  HOH   HOH A . 
F 5 HOH   56 356 39  HOH   HOH A . 
F 5 HOH   57 357 62  HOH   HOH A . 
F 5 HOH   58 358 80  HOH   HOH A . 
F 5 HOH   59 359 54  HOH   HOH A . 
F 5 HOH   60 360 35  HOH   HOH A . 
F 5 HOH   61 361 69  HOH   HOH A . 
F 5 HOH   62 362 77  HOH   HOH A . 
F 5 HOH   63 363 34  HOH   HOH A . 
F 5 HOH   64 364 7   HOH   HOH A . 
F 5 HOH   65 365 63  HOH   HOH A . 
F 5 HOH   66 366 50  HOH   HOH A . 
F 5 HOH   67 367 67  HOH   HOH A . 
F 5 HOH   68 368 30  HOH   HOH A . 
F 5 HOH   69 369 78  HOH   HOH A . 
F 5 HOH   70 370 20  HOH   HOH A . 
F 5 HOH   71 371 51  HOH   HOH A . 
F 5 HOH   72 372 82  HOH   HOH A . 
F 5 HOH   73 373 71  HOH   HOH A . 
F 5 HOH   74 374 64  HOH   HOH A . 
F 5 HOH   75 375 23  HOH   HOH A . 
F 5 HOH   76 376 21  HOH   HOH A . 
F 5 HOH   77 377 74  HOH   HOH A . 
F 5 HOH   78 378 2   HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7HUG 
_cell.length_a           72.704 
_cell.length_b           61.675 
_cell.length_c           32.755 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.97 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HUG 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
_exptl.entry_id          7HUG 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.31 
_exptl_crystal.density_percent_sol   46.69 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-10-03 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92208 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92208 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HUG 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.30 
_reflns.d_resolution_high            1.64 
_reflns.number_obs                   17745 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.144 
_reflns.pdbx_netI_over_sigmaI        8.2 
_reflns.pdbx_redundancy              4.6 
_reflns.pdbx_Rrim_I_all              0.163 
_reflns.pdbx_Rpim_I_all              0.075 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     82302 
_reflns.pdbx_chi_squared             0.94 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.64 
_reflns_shell.d_res_low                   1.73 
_reflns_shell.number_measured_all         12044 
_reflns_shell.number_unique_obs           2582 
_reflns_shell.Rmerge_I_obs                1.084 
_reflns_shell.pdbx_chi_squared            0.69 
_reflns_shell.pdbx_redundancy             4.7 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.3 
_reflns_shell.pdbx_Rrim_I_all             1.224 
_reflns_shell.pdbx_Rpim_I_all             0.561 
_reflns_shell.pdbx_CC_half                0.399 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HUG 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     17730 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             36.30 
_refine.ls_d_res_high                            1.640 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_R_factor_obs                          0.2379 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2360 
_refine.ls_R_factor_R_free                       0.2802 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.530 
_refine.ls_number_reflns_R_free                  803 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.940 
_refine.correlation_coeff_Fo_to_Fc_free          0.896 
_refine.B_iso_mean                               29.23 
_refine.aniso_B[1][1]                            1.74930 
_refine.aniso_B[2][2]                            -2.41380 
_refine.aniso_B[3][3]                            0.66440 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.33420 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.116 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.118 
_refine.pdbx_overall_SU_R_Blow_DPI               0.117 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.118 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HUG 
_refine_analyze.Luzzati_coordinate_error_obs    0.26 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.number_atoms_solvent             78 
_refine_hist.number_atoms_total               1180 
_refine_hist.d_res_high                       1.640 
_refine_hist.d_res_low                        36.30 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  1130 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.03  ? 2.00  1536 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  376  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1130 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.85  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.05 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  931  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   41 
_refine_ls_shell.d_res_high                       1.64 
_refine_ls_shell.d_res_low                        1.66 
_refine_ls_shell.number_reflns_R_work             428 
_refine_ls_shell.R_factor_R_work                  0.3514 
_refine_ls_shell.percent_reflns_obs               98.70 
_refine_ls_shell.R_factor_R_free                  0.3191 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            3.60 
_refine_ls_shell.number_reflns_R_free             16 
_refine_ls_shell.number_reflns_all                444 
_refine_ls_shell.R_factor_all                     0.3503 
# 
_struct.entry_id                  7HUG 
_struct.title                     
;Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre -- Crystal structure of Coxsackievirus A16 (G-10) 2A protease in complex with ASAP-0031501-001 (A71EV2A-x3054)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HUG 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HUG 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6 AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.236 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.322 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.441 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.222 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 118.0 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 108.3 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.2 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 111.0 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 96.0  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 107.3 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N ILE A 117 ? N ILE A 123 O ALA A 129 ? O ALA A 135 
AA2 5 6 O ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HUG 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -132.64 
_pdbx_validate_torsion.psi             -33.05 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     372 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.1189 
_pdbx_refine_tls.origin_y         7.1249 
_pdbx_refine_tls.origin_z         14.2412 
_pdbx_refine_tls.T[1][1]          0.0128 
_pdbx_refine_tls.T[2][2]          -0.0656 
_pdbx_refine_tls.T[3][3]          -0.0364 
_pdbx_refine_tls.T[1][2]          -0.0044 
_pdbx_refine_tls.T[1][3]          -0.0234 
_pdbx_refine_tls.T[2][3]          -0.0101 
_pdbx_refine_tls.L[1][1]          2.3933 
_pdbx_refine_tls.L[2][2]          9.9967 
_pdbx_refine_tls.L[3][3]          0.9611 
_pdbx_refine_tls.L[1][2]          3.9066 
_pdbx_refine_tls.L[1][3]          -1.4472 
_pdbx_refine_tls.L[2][3]          -3.4759 
_pdbx_refine_tls.S[1][1]          -0.1472 
_pdbx_refine_tls.S[1][2]          0.0835 
_pdbx_refine_tls.S[1][3]          0.0523 
_pdbx_refine_tls.S[2][1]          0.3091 
_pdbx_refine_tls.S[2][2]          0.1715 
_pdbx_refine_tls.S[2][3]          -0.2977 
_pdbx_refine_tls.S[3][1]          -0.0415 
_pdbx_refine_tls.S[3][2]          -0.1942 
_pdbx_refine_tls.S[3][3]          -0.0243 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BRE N1   N  N N 1   
A1BRE C4   C  Y N 2   
A1BRE C5   C  Y N 3   
A1BRE C6   C  N N 4   
A1BRE C7   C  N N 5   
A1BRE C8   C  N N 6   
A1BRE C10  C  N S 7   
A1BRE C13  C  Y N 8   
A1BRE O1   O  N N 9   
A1BRE C11  C  N N 10  
A1BRE N2   N  N N 11  
A1BRE C9   C  N N 12  
A1BRE C12  C  N N 13  
A1BRE O    O  N N 14  
A1BRE N    N  N N 15  
A1BRE C3   C  Y N 16  
A1BRE C2   C  Y N 17  
A1BRE C1   C  Y N 18  
A1BRE C    C  N N 19  
A1BRE H6   H  N N 20  
A1BRE H9   H  N N 21  
A1BRE H8   H  N N 22  
A1BRE H10  H  N N 23  
A1BRE H11  H  N N 24  
A1BRE H    H  N N 25  
A1BRE H18  H  N N 26  
A1BRE H15  H  N N 27  
A1BRE H14  H  N N 28  
A1BRE H12  H  N N 29  
A1BRE H13  H  N N 30  
A1BRE H16  H  N N 31  
A1BRE H17  H  N N 32  
A1BRE H7   H  N N 33  
A1BRE H5   H  N N 34  
A1BRE H4   H  N N 35  
A1BRE H2   H  N N 36  
A1BRE H3   H  N N 37  
A1BRE H1   H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
DMS   S    S  N N 126 
DMS   O    O  N N 127 
DMS   C1   C  N N 128 
DMS   C2   C  N N 129 
DMS   H11  H  N N 130 
DMS   H12  H  N N 131 
DMS   H13  H  N N 132 
DMS   H21  H  N N 133 
DMS   H22  H  N N 134 
DMS   H23  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
THR   N    N  N N 352 
THR   CA   C  N S 353 
THR   C    C  N N 354 
THR   O    O  N N 355 
THR   CB   C  N R 356 
THR   OG1  O  N N 357 
THR   CG2  C  N N 358 
THR   OXT  O  N N 359 
THR   H    H  N N 360 
THR   H2   H  N N 361 
THR   HA   H  N N 362 
THR   HB   H  N N 363 
THR   HG1  H  N N 364 
THR   HG21 H  N N 365 
THR   HG22 H  N N 366 
THR   HG23 H  N N 367 
THR   HXT  H  N N 368 
TRP   N    N  N N 369 
TRP   CA   C  N S 370 
TRP   C    C  N N 371 
TRP   O    O  N N 372 
TRP   CB   C  N N 373 
TRP   CG   C  Y N 374 
TRP   CD1  C  Y N 375 
TRP   CD2  C  Y N 376 
TRP   NE1  N  Y N 377 
TRP   CE2  C  Y N 378 
TRP   CE3  C  Y N 379 
TRP   CZ2  C  Y N 380 
TRP   CZ3  C  Y N 381 
TRP   CH2  C  Y N 382 
TRP   OXT  O  N N 383 
TRP   H    H  N N 384 
TRP   H2   H  N N 385 
TRP   HA   H  N N 386 
TRP   HB2  H  N N 387 
TRP   HB3  H  N N 388 
TRP   HD1  H  N N 389 
TRP   HE1  H  N N 390 
TRP   HE3  H  N N 391 
TRP   HZ2  H  N N 392 
TRP   HZ3  H  N N 393 
TRP   HH2  H  N N 394 
TRP   HXT  H  N N 395 
TYR   N    N  N N 396 
TYR   CA   C  N S 397 
TYR   C    C  N N 398 
TYR   O    O  N N 399 
TYR   CB   C  N N 400 
TYR   CG   C  Y N 401 
TYR   CD1  C  Y N 402 
TYR   CD2  C  Y N 403 
TYR   CE1  C  Y N 404 
TYR   CE2  C  Y N 405 
TYR   CZ   C  Y N 406 
TYR   OH   O  N N 407 
TYR   OXT  O  N N 408 
TYR   H    H  N N 409 
TYR   H2   H  N N 410 
TYR   HA   H  N N 411 
TYR   HB2  H  N N 412 
TYR   HB3  H  N N 413 
TYR   HD1  H  N N 414 
TYR   HD2  H  N N 415 
TYR   HE1  H  N N 416 
TYR   HE2  H  N N 417 
TYR   HH   H  N N 418 
TYR   HXT  H  N N 419 
VAL   N    N  N N 420 
VAL   CA   C  N S 421 
VAL   C    C  N N 422 
VAL   O    O  N N 423 
VAL   CB   C  N N 424 
VAL   CG1  C  N N 425 
VAL   CG2  C  N N 426 
VAL   OXT  O  N N 427 
VAL   H    H  N N 428 
VAL   H2   H  N N 429 
VAL   HA   H  N N 430 
VAL   HB   H  N N 431 
VAL   HG11 H  N N 432 
VAL   HG12 H  N N 433 
VAL   HG13 H  N N 434 
VAL   HG21 H  N N 435 
VAL   HG22 H  N N 436 
VAL   HG23 H  N N 437 
VAL   HXT  H  N N 438 
ZN    ZN   ZN N N 439 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BRE C   C1   sing N N 1   
A1BRE C1  C2   doub Y N 2   
A1BRE C2  C3   sing Y N 3   
A1BRE C3  C4   doub Y N 4   
A1BRE C4  C5   sing Y N 5   
A1BRE C5  N    sing N N 6   
A1BRE N   C6   sing N N 7   
A1BRE O   C6   doub N N 8   
A1BRE C6  N1   sing N N 9   
A1BRE N1  C7   sing N N 10  
A1BRE C7  C8   sing N N 11  
A1BRE C8  C9   sing N N 12  
A1BRE C9  C10  sing N N 13  
A1BRE C10 C11  sing N N 14  
A1BRE N2  C11  sing N N 15  
A1BRE C11 O1   doub N N 16  
A1BRE C12 C10  sing N N 17  
A1BRE N1  C12  sing N N 18  
A1BRE C13 C5   doub Y N 19  
A1BRE C1  C13  sing Y N 20  
A1BRE C4  H6   sing N N 21  
A1BRE C7  H9   sing N N 22  
A1BRE C7  H8   sing N N 23  
A1BRE C8  H10  sing N N 24  
A1BRE C8  H11  sing N N 25  
A1BRE C10 H    sing N N 26  
A1BRE C13 H18  sing N N 27  
A1BRE N2  H15  sing N N 28  
A1BRE N2  H14  sing N N 29  
A1BRE C9  H12  sing N N 30  
A1BRE C9  H13  sing N N 31  
A1BRE C12 H16  sing N N 32  
A1BRE C12 H17  sing N N 33  
A1BRE N   H7   sing N N 34  
A1BRE C3  H5   sing N N 35  
A1BRE C2  H4   sing N N 36  
A1BRE C   H2   sing N N 37  
A1BRE C   H3   sing N N 38  
A1BRE C   H1   sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TRP   N   CA   sing N N 354 
TRP   N   H    sing N N 355 
TRP   N   H2   sing N N 356 
TRP   CA  C    sing N N 357 
TRP   CA  CB   sing N N 358 
TRP   CA  HA   sing N N 359 
TRP   C   O    doub N N 360 
TRP   C   OXT  sing N N 361 
TRP   CB  CG   sing N N 362 
TRP   CB  HB2  sing N N 363 
TRP   CB  HB3  sing N N 364 
TRP   CG  CD1  doub Y N 365 
TRP   CG  CD2  sing Y N 366 
TRP   CD1 NE1  sing Y N 367 
TRP   CD1 HD1  sing N N 368 
TRP   CD2 CE2  doub Y N 369 
TRP   CD2 CE3  sing Y N 370 
TRP   NE1 CE2  sing Y N 371 
TRP   NE1 HE1  sing N N 372 
TRP   CE2 CZ2  sing Y N 373 
TRP   CE3 CZ3  doub Y N 374 
TRP   CE3 HE3  sing N N 375 
TRP   CZ2 CH2  doub Y N 376 
TRP   CZ2 HZ2  sing N N 377 
TRP   CZ3 CH2  sing Y N 378 
TRP   CZ3 HZ3  sing N N 379 
TRP   CH2 HH2  sing N N 380 
TRP   OXT HXT  sing N N 381 
TYR   N   CA   sing N N 382 
TYR   N   H    sing N N 383 
TYR   N   H2   sing N N 384 
TYR   CA  C    sing N N 385 
TYR   CA  CB   sing N N 386 
TYR   CA  HA   sing N N 387 
TYR   C   O    doub N N 388 
TYR   C   OXT  sing N N 389 
TYR   CB  CG   sing N N 390 
TYR   CB  HB2  sing N N 391 
TYR   CB  HB3  sing N N 392 
TYR   CG  CD1  doub Y N 393 
TYR   CG  CD2  sing Y N 394 
TYR   CD1 CE1  sing Y N 395 
TYR   CD1 HD1  sing N N 396 
TYR   CD2 CE2  doub Y N 397 
TYR   CD2 HD2  sing N N 398 
TYR   CE1 CZ   doub Y N 399 
TYR   CE1 HE1  sing N N 400 
TYR   CE2 CZ   sing Y N 401 
TYR   CE2 HE2  sing N N 402 
TYR   CZ  OH   sing N N 403 
TYR   OH  HH   sing N N 404 
TYR   OXT HXT  sing N N 405 
VAL   N   CA   sing N N 406 
VAL   N   H    sing N N 407 
VAL   N   H2   sing N N 408 
VAL   CA  C    sing N N 409 
VAL   CA  CB   sing N N 410 
VAL   CA  HA   sing N N 411 
VAL   C   O    doub N N 412 
VAL   C   OXT  sing N N 413 
VAL   CB  CG1  sing N N 414 
VAL   CB  CG2  sing N N 415 
VAL   CB  HB   sing N N 416 
VAL   CG1 HG11 sing N N 417 
VAL   CG1 HG12 sing N N 418 
VAL   CG1 HG13 sing N N 419 
VAL   CG2 HG21 sing N N 420 
VAL   CG2 HG22 sing N N 421 
VAL   CG2 HG23 sing N N 422 
VAL   OXT HXT  sing N N 423 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HUG 
_atom_sites.fract_transf_matrix[1][1]   0.013754 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000714 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016214 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.030571 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.899 6.509   24.289 1.00 32.20 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.067 6.656   23.424 1.00 32.19 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.153 5.494   22.414 1.00 30.04 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.491 4.457   22.589 1.00 30.00 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.329 6.708   24.275 1.00 34.39 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.452 5.456   24.935 1.00 37.40 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.978 5.676   21.387 1.00 27.87 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.202 4.673   20.357 1.00 26.44 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.437 5.248   18.978 1.00 25.49 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.994 6.363   18.680 1.00 23.99 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.162 4.507   18.144 1.00 24.63 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.468 4.936   16.780 1.00 24.66 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.458 3.735   15.806 1.00 24.81 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.523 2.589   16.260 1.00 25.12 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.842 5.582   16.760 1.00 24.47 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.442 4.003   14.480 1.00 24.33 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.585 3.028   13.396 1.00 24.60 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.991 3.282   12.779 1.00 27.41 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.343 4.415   12.473 1.00 26.40 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.506 3.231   12.301 1.00 23.53 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.088 3.251   12.875 1.00 23.11 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.645 2.169   11.211 1.00 23.51 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.075 3.720   11.943 1.00 23.27 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.786 2.244   12.617 1.00 30.06 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.127 2.340   12.034 1.00 32.24 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.120 1.576   10.716 1.00 34.71 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.006 0.367   10.745 1.00 35.98 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.159 1.704   12.988 1.00 32.48 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.272 2.459   14.285 1.00 32.85 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.141 3.533   14.411 1.00 34.32 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.418 2.191   15.343 1.00 33.74 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.167 4.311   15.559 1.00 35.19 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.426 2.971   16.492 1.00 34.83 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.330 4.006   16.611 1.00 35.91 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.384 4.756   17.754 1.00 37.97 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.184 2.257   9.576  1.00 36.09 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.183 1.596   8.270  1.00 38.07 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.335 2.180   7.447  1.00 39.85 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.409 3.389   7.262  1.00 40.49 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.818 1.729   7.554  1.00 39.21 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.316 3.182   7.563  1.00 39.33 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.893 1.187   6.141  1.00 40.21 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.288 1.341   7.034  1.00 41.00 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.466 1.809   6.313  1.00 41.97 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.243 2.828   7.133  1.00 43.45 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.414 2.629   8.340  1.00 44.23 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.582 3.979   6.543  1.00 43.39 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.276 5.039   7.287  1.00 43.16 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.308 6.083   7.864  1.00 40.11 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.706 7.233   8.086  1.00 39.93 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.313 5.708   6.419  1.00 47.03 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.555 4.890   6.178  1.00 55.24 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.937 4.017   6.960  1.00 57.14 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.246 5.195   5.088  1.00 58.98 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.054 5.678   8.152  1.00 37.48 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.053 6.603   8.685  1.00 35.59 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.522 6.177   10.035 1.00 32.30 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.393 4.999   10.326 1.00 31.49 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.854 6.721   7.720  1.00 35.28 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.215 7.289   6.366  1.00 35.51 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.746 8.561   6.245  1.00 36.49 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.927 6.595   5.202  1.00 36.23 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.063 9.094   5.003  1.00 38.05 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.239 7.114   3.953  1.00 37.61 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.805 8.369   3.856  1.00 39.25 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.106 8.906   2.621  1.00 42.24 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.172 7.160   10.847 1.00 29.92 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.506 6.959   12.129 1.00 27.56 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.224 7.795   12.047 1.00 24.93 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.278 8.962   11.708 1.00 25.26 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.404 7.395   13.290 1.00 27.92 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.689 7.718   14.601 1.00 28.94 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.716 7.998   15.685 1.00 31.39 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.282 9.043   16.608 1.00 33.61 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.735 8.814   17.799 1.00 35.40 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.512 7.567   18.209 1.00 33.56 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.377 9.831   18.578 1.00 35.28 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.062 7.179   12.296 1.00 22.21 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.770 7.859   12.235 1.00 20.28 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.264 7.997   13.646 1.00 19.65 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.126 6.990   14.315 1.00 20.31 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.751 7.082   11.381 1.00 19.21 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.471 7.920   11.177 1.00 18.42 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.363 6.649   10.036 1.00 18.74 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.961 9.206   14.107 1.00 18.02 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.466 9.420   15.470 1.00 17.96 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.244 10.351  15.432 1.00 15.83 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.087 11.115  14.482 1.00 15.74 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.534 10.075  16.400 1.00 19.98 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.431 9.044   17.036 1.00 22.55 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.317 11.185  15.689 1.00 20.49 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.456 10.412  16.534 1.00 13.67 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.426 11.457  16.697 1.00 13.37 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.165 12.797  16.680 1.00 15.29 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.171 12.925  17.373 1.00 16.78 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.752 11.351  18.065 1.00 12.58 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.940 10.088  18.162 1.00 15.94 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.440 9.057   18.594 1.00 17.84 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.692 10.133  17.715 1.00 14.18 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.728 13.748  15.872 1.00 14.72 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.392 15.059  15.813 1.00 14.33 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.441 15.751  17.178 1.00 17.02 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.471 16.362  17.495 1.00 17.47 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.741 15.940  14.743 1.00 14.03 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.512 17.224  14.376 1.00 13.61 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.560 18.076  13.611 1.00 12.24 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.141 19.324  13.068 1.00 12.69 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.203 20.466  13.741 1.00 16.88 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.797 20.522  15.006 1.00 17.65 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.644 21.567  13.149 1.00 15.31 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.379 15.610  18.014 1.00 16.95 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.346 16.243  19.338 1.00 19.48 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.362 15.649  20.344 1.00 22.31 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.762 16.317  21.317 1.00 23.00 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.916 16.260  19.894 1.00 20.08 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.387 14.954  20.409 1.00 19.49 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.787 14.031  19.566 1.00 20.67 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.292 14.506  21.687 1.00 19.13 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.399 13.029  20.345 1.00 20.95 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.674 13.270  21.631 1.00 20.82 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.862 14.451  20.060 1.00 23.09 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.858 13.819  20.903 1.00 24.05 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.278 13.844  20.284 1.00 26.17 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.180 13.219  20.848 1.00 26.76 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.430 12.363  21.196 1.00 23.49 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.145 12.204  22.022 1.00 24.18 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.796 10.742  22.231 1.00 24.17 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.273 12.902  23.397 1.00 24.08 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.480 14.488  19.115 1.00 26.78 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.799 14.484  18.474 1.00 27.87 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.846 15.148  19.364 1.00 29.39 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.521 16.106  20.056 1.00 29.62 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.735 15.176  17.120 1.00 28.19 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.082 14.630  19.364 1.00 30.83 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.196 15.149  20.184 1.00 33.31 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.034 16.248  19.441 1.00 34.44 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.760 16.532  18.283 1.00 34.04 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.102 13.967  20.554 1.00 35.57 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.772 13.544  19.368 1.00 37.49 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.352 12.816  21.187 1.00 36.07 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.091 16.823  20.082 1.00 36.06 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.964 17.776  19.407 1.00 38.09 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.690 17.085  18.252 1.00 38.03 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.825 17.675  17.187 1.00 37.80 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.998 18.339  20.395 1.00 41.21 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.415 19.308  21.365 1.00 47.50 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.655 20.373  20.940 1.00 50.95 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.530 19.362  22.713 1.00 50.37 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.334 21.047  22.034 1.00 52.16 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.846 20.482  23.125 1.00 52.09 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.137 15.827  18.471 1.00 38.06 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.836 14.978  17.493 1.00 38.81 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.976 14.815  16.250 1.00 35.89 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.469 15.034  15.150 1.00 36.55 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.151 13.569  18.057 1.00 42.81 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 32.681 13.490  19.465 1.00 51.83 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 32.866 14.500  20.140 1.00 54.33 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.951 12.250  19.950 1.00 54.68 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.695 14.437  16.420 1.00 33.27 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.723 14.326  15.320 1.00 30.21 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.654 15.613  14.489 1.00 29.01 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.723 15.550  13.267 1.00 28.43 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.320 13.991  15.875 1.00 29.04 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.202 12.566  16.376 1.00 31.11 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.741 11.668  15.715 1.00 31.18 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.577 12.360  17.439 1.00 31.37 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.520 16.778  15.139 1.00 28.75 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.417 18.042  14.411 1.00 28.49 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.688 18.431  13.694 1.00 30.80 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.623 19.070  12.646 1.00 31.10 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.951 19.167  15.332 1.00 27.50 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.461 19.208  15.479 1.00 25.35 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.728 18.720  16.520 1.00 25.88 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.527 19.732  14.538 1.00 23.08 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.394 18.968  16.311 1.00 25.49 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.241 19.583  15.096 1.00 23.90 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.647 20.311  13.272 1.00 22.40 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.097 20.029  14.454 1.00 22.33 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.518 20.788  12.657 1.00 22.07 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.254 20.603  13.226 1.00 21.88 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.848 18.082  14.278 1.00 32.46 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.169 18.374  13.701 1.00 35.63 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.511 17.451  12.516 1.00 37.79 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.467 17.720  11.784 1.00 39.65 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.251 18.225  14.774 1.00 35.44 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.794 16.325  12.397 1.00 36.44 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.927 15.338  11.338 1.00 35.61 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.590 15.170  10.591 1.00 32.32 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.299 14.095  10.098 1.00 31.27 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.325 14.033  11.959 1.00 38.30 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.759 14.005  12.395 1.00 44.11 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.647 14.322  11.616 1.00 46.00 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.013 13.556  13.623 1.00 45.40 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.773 16.236  10.540 1.00 30.14 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.469 16.255  9.902  1.00 27.58 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.511 15.853  8.420  1.00 27.92 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.336 16.387  7.682  1.00 29.66 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.904 17.688  10.020 1.00 25.18 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.503 17.926  9.396  1.00 23.09 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.422 17.191  10.177 1.00 23.17 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.151 19.413  9.359  1.00 21.09 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.570 14.982  7.977  1.00 25.22 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.330 14.606  6.586  1.00 24.04 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.988 15.283  6.137  1.00 23.16 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.936 16.003  5.132  1.00 24.37 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.232 13.070  6.436  1.00 25.82 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.654 12.695  5.074  1.00 27.08 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.588 12.401  6.661  1.00 26.63 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.916 15.090  6.929  1.00 20.54 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.610 15.634  6.614  1.00 18.55 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.737 15.674  7.881  1.00 16.94 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.835 14.801  8.732  1.00 16.59 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.973 14.732  5.529  1.00 17.73 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.494 14.888  5.321  1.00 16.76 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.860 15.750  4.471  1.00 17.69 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.472 14.122  5.955  1.00 15.59 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.496 15.559  4.537  1.00 17.67 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.233 14.567  5.448  1.00 16.85 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.484 13.110  6.916  1.00 14.86 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.020 14.002  5.849  1.00 16.83 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.284 12.550  7.303  1.00 14.99 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.075 12.989  6.766  1.00 15.61 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.904 16.687  7.997  1.00 15.58 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.001 16.824  9.127  1.00 14.36 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.676 17.365  8.648  1.00 14.44 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.623 18.116  7.665  1.00 14.61 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.627 17.649  10.288 1.00 15.41 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.132 19.037  9.915  1.00 16.67 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.059 20.102  9.824  1.00 19.54 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.242 21.102  9.084  1.00 23.54 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.021 19.928  10.496 1.00 18.41 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.598 16.989  9.333  1.00 13.57 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.276 17.486  8.975  1.00 13.75 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.411 17.607  10.246 1.00 13.98 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.968 16.593  10.807 1.00 14.18 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.676 16.657  7.839  1.00 14.88 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.351 17.157  7.329  1.00 21.21 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.680 17.915  8.057  1.00 21.43 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.962 16.756  6.225  1.00 25.38 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.202 18.869  10.723 1.00 14.24 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.407 19.160  11.933 0.50 14.79 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.423 19.109  11.946 0.50 14.67 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.990 18.635  11.808 1.00 15.09 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.418 18.155  12.784 1.00 15.25 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.347 20.664  12.207 0.50 16.09 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.472 20.580  12.362 0.50 15.61 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 16.630 21.258  12.151 0.50 18.50 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.166 21.417  11.263 0.50 17.30 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.414 18.732  10.598 1.00 15.39 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.053 18.283  10.396 1.00 16.14 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.913 16.764  10.564 1.00 15.23 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.815 16.323  10.827 1.00 16.38 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.519 18.756  9.051  1.00 19.67 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.065 17.967  8.009  1.00 24.03 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.009 15.985  10.426 1.00 12.23 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.988 14.518  10.630 1.00 10.60 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.595 14.081  11.935 1.00 11.79 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.570 12.881  12.233 1.00 12.48 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.708 13.777  9.488  1.00 11.58 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.126 14.123  8.131  1.00 12.99 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.837 13.415  6.971  1.00 14.71 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.838 11.954  7.109  1.00 13.48 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.020 11.106  6.092  1.00 15.29 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.056 11.554  4.842  1.00 14.28 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.053 9.792   6.310  1.00 17.02 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.253 15.016  12.668 1.00 11.83 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.978 14.732  13.912 1.00 11.91 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.100 13.746  13.596 1.00 12.22 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.381 12.885  14.421 1.00 10.90 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.045 14.179  15.007 1.00 12.21 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.750 13.879  16.340 1.00 15.87 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.550 14.707  16.783 1.00 14.78 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.507 12.792  16.921 1.00 18.41 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.731 13.828  12.390 1.00 12.37 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.862 12.929  12.054 1.00 11.21 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.152 13.717  11.837 1.00 12.86 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.127 14.846  11.358 1.00 14.79 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.620 12.109  10.770 1.00 10.79 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.602 10.963  10.874 1.00 11.57 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.505 10.214  9.528  1.00 11.11 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.992 9.955   11.973 1.00 11.93 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.278 13.091  12.153 1.00 12.72 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.576 13.656  11.879 1.00 14.32 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.470 12.471  11.536 1.00 15.00 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.382 11.413  12.176 1.00 15.18 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.146 14.489  13.069 1.00 14.33 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.550 15.092  12.823 1.00 16.23 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.718 16.406  13.504 1.00 17.47 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.709 14.157  13.245 1.00 16.60 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.282 12.611  10.466 1.00 15.93 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.242 11.584  10.040 1.00 17.35 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.633 12.205  10.143 1.00 19.76 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.824 13.326  9.679  1.00 18.89 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.975 11.053  8.597  1.00 18.97 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.046 10.021  8.186  1.00 20.20 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.563 10.431  8.500  1.00 19.37 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.577 11.492  10.767 1.00 22.94 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.971 11.920  10.887 1.00 26.21 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.894 10.811  10.371 1.00 30.65 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.521 9.634   10.362 1.00 29.30 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.320 12.288  12.326 1.00 26.27 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.115 11.202  13.220 1.00 27.48 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.110 11.189  9.963  1.00 34.24 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.091 10.247  9.438  1.00 39.00 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.850 9.534   10.549 1.00 43.23 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.114 10.118  11.596 1.00 42.94 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.093 10.980  8.554  1.00 40.55 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.572 12.127  9.238  1.00 43.66 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.249 8.287   10.303 1.00 47.17 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.989 7.499   11.290 1.00 51.39 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.294 6.989   10.692 1.00 57.53 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.419 6.908   9.470  1.00 58.90 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.154 6.300   11.791 1.00 51.77 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.066 5.313   10.766 1.00 52.90 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.776 6.687   12.285 1.00 51.49 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.246 6.596   11.547 1.00 60.70 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.517 6.040   11.090 1.00 63.89 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.392 4.506   10.942 1.00 66.81 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.023 3.911   10.072 1.00 69.03 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.637 6.458   12.057 1.00 65.21 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.245 6.049   13.371 1.00 66.25 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.864 7.968   12.062 1.00 65.38 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.581 3.859   11.792 1.00 66.46 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.374 2.418   11.754 1.00 66.43 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.219 2.038   10.804 1.00 66.24 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.404 2.897   10.447 1.00 66.50 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.091 1.914   13.165 1.00 66.76 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.143 0.752   10.400 1.00 65.94 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.096 0.239   9.513  1.00 65.46 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.838 -0.179  10.248 1.00 63.95 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 31.900 -0.920  11.229 1.00 64.26 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.591 -0.995  8.739  1.00 67.55 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.888 -1.173  7.401  1.00 71.34 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.473 -0.167  6.446  1.00 76.68 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.687 -0.071  6.315  1.00 79.19 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.642 0.626   5.780  1.00 77.67 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.703 0.200   9.680  1.00 61.87 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.377 -0.141  10.172 1.00 59.87 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.794 -1.303  9.392  1.00 56.88 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 28.835 -1.318  8.159  1.00 56.23 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.234 -2.260  10.097 1.00 55.15 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.696 -3.452  9.455  1.00 54.28 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.174 -3.582  9.531  1.00 51.40 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.647 -4.634  9.159  1.00 51.63 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.390 -4.691  10.000 1.00 56.89 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.186 -4.672  9.799  1.00 65.49 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.462 -2.527  9.987  1.00 48.14 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.005 -2.578  10.042 1.00 45.92 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.475 -2.547  8.622  1.00 43.76 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 23.949 -1.786  7.790  1.00 44.57 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.409 -1.383  10.830 1.00 47.47 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.375 -1.521  12.340 1.00 50.33 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.100 -2.632  12.829 1.00 51.27 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.603 -0.513  13.031 1.00 50.93 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.488 -3.345  8.357  1.00 41.87 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.851 -3.434  7.055  1.00 40.54 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.599 -2.571  7.121  1.00 37.92 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.823 -2.709  8.060  1.00 38.50 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.565 -4.925  6.756  1.00 42.51 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.764 -5.518  6.219  1.00 45.14 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.384 -5.135  5.806  1.00 41.60 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.422 -1.662  6.171  1.00 35.12 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.236 -0.824  6.131  1.00 33.24 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.195 -1.532  5.281  1.00 32.10 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.521 -2.035  4.190  1.00 31.86 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.521 0.591   5.574  1.00 33.02 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.711 1.269   6.280  1.00 32.84 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.262 1.463   5.613  1.00 33.07 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.507 1.480   7.771  1.00 32.47 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.959 -1.590  5.769  1.00 29.85 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.879 -2.189  5.019  1.00 29.40 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.415 -1.281  3.878  1.00 29.29 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.312 -0.083  4.042  1.00 28.40 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.712 -2.504  5.942  1.00 28.55 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.110 -1.861  2.733  1.00 30.56 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.590 -1.138  1.574  1.00 32.20 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.271 -1.847  1.275  1.00 33.55 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.265 -2.933  0.650  1.00 34.91 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.573 -1.246  0.396  1.00 33.73 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.936 -0.627  0.658  1.00 34.84 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.945 0.870   1.086  1.00 36.01 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.309 1.307   1.389  1.00 35.34 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.621 2.400   2.081  1.00 34.63 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.669 3.201   2.534  1.00 31.95 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.888 2.696   2.326  1.00 34.33 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.154 -1.288  1.812  1.00 32.30 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.858 -1.959  1.735  1.00 32.32 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.705  -1.015  2.191  1.00 33.15 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.943  0.119   2.599  1.00 31.58 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.923 -3.176  2.655  1.00 31.82 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.054 -2.736  4.427  1.00 29.67 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.457  -1.558  2.236  1.00 34.62 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.280  -0.840  2.738  1.00 35.36 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.588  -1.640  3.851  1.00 34.01 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.373  -1.577  3.988  1.00 34.99 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.299  -0.416  1.595  1.00 39.46 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.436  -1.497  0.978  1.00 48.99 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.661  -2.685  1.281  1.00 51.34 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.527  -1.152  0.180  1.00 54.31 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.371  -2.421  4.625  1.00 31.79 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.933  -3.221  5.786  1.00 29.42 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.241  -2.319  6.767  1.00 27.37 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.700  -1.213  6.991  1.00 28.47 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.131  -3.873  6.473  1.00 29.22 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.618  -5.469  5.790  1.00 30.59 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.169  -2.780  7.350  1.00 24.37 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.438  -2.073  8.392  1.00 22.18 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.418  -2.877  9.673  1.00 19.20 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.579  -2.610  10.523 1.00 18.87 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 2.984  -1.716  7.958  1.00 24.45 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 2.857  -0.408  7.146  1.00 30.24 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.408  -0.000  6.878  1.00 34.87 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 0.915  -0.061  5.747  1.00 37.46 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.691  0.435   7.911  1.00 33.80 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.257  -3.940  9.805  1.00 17.73 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.356  -4.722  11.049 1.00 16.20 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.852  -4.940  11.287 1.00 14.08 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.648  -5.026  10.346 1.00 14.78 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.619  -6.078  11.004 1.00 20.00 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.325  -6.940  10.127 1.00 23.68 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.146  -5.979  10.585 1.00 20.14 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.228  -4.999  12.544 1.00 12.21 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.616  -5.181  12.918 1.00 11.51 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.755  -5.307  14.422 1.00 11.42 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.760  -5.521  15.104 1.00 12.29 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.978  -5.149  14.947 1.00 10.48 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.253 -5.258  16.395 1.00 10.59 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.145 -4.058  16.783 1.00 9.92  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.105 -3.766  16.063 1.00 8.84  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 10.979 -6.619  16.659 1.00 11.89 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.321 -6.819  18.135 1.00 12.81 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.144 -7.794  16.137 1.00 11.50 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.856 -3.411  17.909 1.00 10.10 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.727 -2.323  18.377 1.00 9.08  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.306 -2.603  19.753 1.00 10.52 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.734 -3.365  20.526 1.00 10.74 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.042 -0.929  18.315 1.00 8.71  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.056 -0.697  19.450 1.00 10.06 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.796  -1.294  19.442 1.00 11.43 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.374 0.133   20.519 1.00 11.65 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.859  -1.019  20.438 1.00 13.44 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.457  0.384   21.546 1.00 13.57 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.210  -0.221  21.517 1.00 15.31 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.288  0.020   22.522 1.00 18.65 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.441 -1.991  20.043 1.00 10.56 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.066 -2.133  21.342 1.00 12.84 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.623 -0.997  22.261 1.00 13.40 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.673 0.193   21.867 1.00 11.90 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.589 -2.221  21.255 1.00 14.51 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.202 -2.338  22.641 1.00 17.17 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.960 -3.447  23.434 1.00 19.08 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.932 -1.296  23.190 1.00 19.28 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.515 -3.560  24.711 1.00 21.37 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.455 -1.377  24.477 1.00 21.91 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.224 -2.504  25.240 1.00 23.88 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.715 -2.575  26.518 1.00 28.67 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.097 -1.364  23.456 1.00 14.97 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.607 -0.369  24.428 1.00 17.55 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.486 -0.397  25.706 1.00 20.51 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.336 -1.292  26.550 1.00 20.41 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.135 -0.626  24.735 1.00 18.85 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.460 0.340   26.119 1.00 21.54 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.462 0.522   25.794 1.00 22.80 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.396 0.537   26.924 1.00 26.02 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.748 0.726   28.282 1.00 27.62 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.233 0.137   29.263 1.00 29.19 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.499 1.572   26.725 1.00 30.39 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.976 2.866   26.495 1.00 36.02 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.638 1.487   28.357 1.00 28.09 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.898 1.720   29.618 1.00 29.78 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.216 0.449   30.200 1.00 30.38 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.703 0.463   31.334 1.00 32.23 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.897 2.863   29.475 1.00 30.79 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.773 2.525   28.679 1.00 31.59 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.244 -0.639  29.433 1.00 28.77 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.734 -1.938  29.819 1.00 28.22 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.776 -3.050  29.624 1.00 29.20 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.481 -4.209  29.950 1.00 29.77 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.520 -2.290  28.951 1.00 26.62 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.271  -1.463  29.216 1.00 29.29 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.668  -1.723  30.589 1.00 33.15 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.441  -0.954  30.801 1.00 35.48 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.391  0.236   31.388 1.00 38.54 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.504  0.814   31.834 1.00 38.31 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.225  0.849   31.560 1.00 38.73 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.964 -2.737  29.049 1.00 28.85 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.009 -3.700  28.689 1.00 28.93 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.389 -4.880  27.893 1.00 26.39 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.659 -6.047  28.188 1.00 26.52 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.808 -4.156  29.923 1.00 32.24 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.677 -3.065  30.520 1.00 39.51 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.576 -3.659  31.591 1.00 47.78 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.070 -2.645  32.517 1.00 56.34 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.976 -2.732  33.841 1.00 62.65 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.389 -3.785  34.406 1.00 63.28 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.450 -1.758  34.611 1.00 65.21 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.481 -4.553  26.931 1.00 23.48 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.714 -5.562  26.165 1.00 21.51 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.485 -5.147  24.714 1.00 18.45 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.430 -3.965  24.430 1.00 18.32 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.305 -5.749  26.783 1.00 23.71 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.198 -6.842  27.836 1.00 30.09 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.910  -6.701  28.649 1.00 36.89 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.754  -7.855  29.619 1.00 41.68 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.173  -7.433  30.929 1.00 44.87 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.302 -6.133  23.822 1.00 15.61 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.953 -5.900  22.428 1.00 13.90 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.457 -6.144  22.316 1.00 14.11 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.915  -7.094  22.933 1.00 14.56 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.703 -6.864  21.480 1.00 14.20 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.192 -6.716  21.523 1.00 13.83 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.873 -5.916  20.596 1.00 16.24 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.083 -7.198  22.405 1.00 14.30 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.144 -5.987  20.930 1.00 15.58 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.321 -6.728  22.014 1.00 15.63 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.774  -5.296  21.547 1.00 12.37 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.336  -5.485  21.364 1.00 12.59 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.962  -5.551  19.896 1.00 12.00 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.439  -4.745  19.105 1.00 10.33 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.575  -4.300  22.001 1.00 13.37 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.626  -4.267  23.511 1.00 15.10 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.845  -5.133  24.277 1.00 16.28 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.356  -3.296  24.176 1.00 16.79 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.881  -5.091  25.676 1.00 17.69 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.403  -3.251  25.565 1.00 18.37 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.647  -4.132  26.310 1.00 18.86 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.656  -4.027  27.685 1.00 23.49 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.096  -6.509  19.504 1.00 12.74 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.596  -6.522  18.108 1.00 12.98 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.538  -5.392  17.924 1.00 15.00 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.713  -5.181  18.832 1.00 16.08 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.922  -7.892  17.984 1.00 14.19 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.492  -8.226  19.413 1.00 15.38 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.461  -7.542  20.355 1.00 13.06 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.573  -4.674  16.799 1.00 13.98 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.645  -3.566  16.499 1.00 15.19 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.176  -3.580  15.065 1.00 15.47 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.928  -3.964  14.159 1.00 16.04 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.272  -2.148  16.718 1.00 16.76 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.205  -1.709  18.175 1.00 18.21 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.687  -2.039  16.131 1.00 17.18 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.954  -3.075  14.842 1.00 15.60 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.444  -2.700  13.539 1.00 17.03 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.634  -1.189  13.571 1.00 17.33 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.356  -0.573  14.605 1.00 19.76 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.951  -2.971  13.414 1.00 19.20 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.743  -4.371  13.468 1.00 24.02 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.188  -0.612  12.526 1.00 15.19 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.409  0.823   12.493 1.00 15.77 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.853  1.440   11.228 1.00 19.08 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.544  0.720   10.267 1.00 20.81 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.896  1.159   12.740 1.00 14.57 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.859  0.413   11.840 1.00 13.21 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.354  -0.827  12.205 1.00 12.83 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.283  0.965   10.639 1.00 14.34 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.298  -1.473  11.404 1.00 14.36 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.169  0.290   9.818  1.00 15.41 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.644  -0.950  10.187 1.00 15.04 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.634  2.783   11.229 1.00 19.75 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.045  3.428   10.085 1.00 21.15 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.120  3.785   9.003  1.00 21.14 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.312  3.650   9.243  1.00 20.39 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.263  4.662   10.541 1.00 24.06 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.163  5.595   11.126 1.00 26.30 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.704  4.205   7.810  1.00 22.63 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.634  4.612   6.745  1.00 24.80 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.241  5.970   7.092  1.00 25.90 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.588  6.742   7.797  1.00 26.42 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.904  4.635   5.385  1.00 28.40 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.530  3.206   4.962  1.00 33.04 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.160  3.033   3.448  1.00 41.48 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.152  1.535   3.173  1.00 48.37 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.591  1.170   1.848  1.00 52.68 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.490  6.286   6.670  1.00 26.55 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.076  7.577   7.064  1.00 27.33 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.231  8.760   6.598  1.00 28.91 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.644  8.733   5.505  1.00 29.06 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.490  7.561   6.457  1.00 27.95 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.506  6.473   5.466  1.00 28.21 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.425  5.479   5.860  1.00 26.19 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.040  9.729   7.493  1.00 29.63 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.190  10.881  7.196  1.00 31.08 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.495  12.053  8.136  1.00 31.27 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.386  11.955  8.976  1.00 29.86 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.706  10.488  7.235  1.00 34.16 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.315  10.035  8.521  1.00 38.17 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.837  13.206  7.903  1.00 32.52 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.998  14.424  8.688  1.00 34.02 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.083  14.290  9.857  1.00 34.73 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.877  14.259  9.647  1.00 36.97 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.477  15.627  7.890  1.00 34.83 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.402  16.221  6.907  1.00 36.81 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.633  17.151  5.985  1.00 38.53 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.503  16.955  7.618  1.00 37.20 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.614  14.310  11.072 1.00 33.80 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.804  14.204  12.274 1.00 34.13 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.138  15.370  13.216 1.00 35.68 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.304  15.670  13.393 1.00 33.90 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.043  12.802  12.919 1.00 33.84 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.275  11.709  12.151 1.00 34.56 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.699  12.776  14.404 1.00 34.12 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.777  10.352  12.325 1.00 35.90 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.118  16.058  13.798 1.00 38.43 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.404  17.174  14.721 1.00 41.54 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.083  16.690  16.046 1.00 41.19 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.642  15.732  16.657 1.00 41.37 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.121  17.977  15.017 1.00 44.37 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.295  19.145  15.957 1.00 47.28 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.844  20.332  15.517 1.00 48.75 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.871  19.065  17.272 1.00 49.56 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.986  21.411  16.379 1.00 49.97 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.993  20.159  18.126 1.00 50.58 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.568  21.314  17.679 1.00 50.08 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.162  17.354  16.462 1.00 41.20 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.913  17.061  17.674 1.00 42.00 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.956  18.301  18.583 1.00 43.67 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.387  19.395  18.173 1.00 42.26 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.343  16.526  17.360 1.00 42.18 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.072  16.105  18.633 1.00 42.64 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.294  15.368  16.378 1.00 42.29 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.507  18.107  19.823 1.00 45.63 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.444  19.112  20.887 1.00 47.46 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.830  19.697  21.164 1.00 47.58 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.833  18.987  21.039 1.00 47.53 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.933  18.426  22.161 1.00 51.86 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.423  18.432  22.313 1.00 60.85 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.875  19.605  23.104 1.00 70.63 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 2.609  20.603  23.291 1.00 71.48 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.701  19.527  23.532 1.00 74.19 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.893  20.980  21.556 1.00 47.33 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.168  21.635  21.866 1.00 47.55 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.009  20.904  22.941 1.00 47.69 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.467  20.185  23.784 1.00 48.56 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.924  23.074  22.284 1.00 47.53 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.331  21.075  22.888 1.00 46.49 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.286 20.470  23.818 1.00 45.34 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.505 21.409  23.988 1.00 45.08 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.586 22.438  23.299 1.00 44.44 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.743 19.115  23.278 1.00 45.69 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.459 19.262  22.061 1.00 46.99 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.472 21.063  24.876 1.00 44.79 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.688 21.896  24.993 1.00 45.21 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.605 21.794  23.758 1.00 41.99 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.658 22.425  23.716 1.00 42.08 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.494 21.588  26.276 1.00 51.24 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.675 21.191  27.497 1.00 59.49 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 13.586 19.689  27.689 1.00 68.85 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 13.626 18.952  26.675 1.00 68.00 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 13.481 19.251  28.859 1.00 74.64 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.222 20.966  22.770 1.00 38.99 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 14.974 20.753  21.557 1.00 36.22 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.293 21.453  20.377 1.00 33.75 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.980 21.974  19.502 1.00 33.86 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.072 19.242  21.287 1.00 34.98 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.581 18.447  22.466 1.00 34.79 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 16.911 18.513  22.856 1.00 35.97 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.734 17.620  23.188 1.00 35.76 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.387 17.767  23.934 1.00 37.37 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.192 16.884  24.274 1.00 37.14 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.523 16.946  24.637 1.00 38.73 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.971 16.190  25.706 1.00 41.63 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.960 21.430  20.323 1.00 31.54 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.244 22.011  19.184 1.00 30.41 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.004 22.772  19.570 1.00 33.52 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.318 22.377  20.506 1.00 34.35 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.752 20.873  18.258 1.00 27.15 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.809 19.946  17.735 1.00 23.26 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 12.841 18.611  18.119 1.00 21.80 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.714 20.368  16.772 1.00 22.62 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 13.792 17.741  17.620 1.00 20.72 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.661 19.499  16.251 1.00 21.70 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.688 18.181  16.669 1.00 20.67 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.645 17.320  16.177 1.00 16.99 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.599 23.773  18.765 1.00 35.17 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.272  24.390  18.998 1.00 36.61 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.171  23.408  18.504 1.00 38.62 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.484  22.389  17.872 1.00 38.06 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.328  25.638  18.110 1.00 37.12 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.202 25.242  16.978 1.00 36.79 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.255 24.310  17.553 1.00 34.41 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.872  23.726  18.719 1.00 40.32 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.770  22.890  18.200 1.00 41.30 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.885  22.851  16.647 1.00 39.62 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.170  23.884  16.053 1.00 39.43 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.432  23.502  18.606 1.00 42.97 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.780  21.661  16.015 1.00 37.44 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.003  21.571  14.554 1.00 35.27 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.506  20.228  13.971 1.00 34.53 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.201  19.318  14.737 1.00 34.88 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.522  21.728  14.269 1.00 33.69 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.342  20.404  14.432 1.00 33.50 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.747  20.591  14.964 1.00 32.38 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.631 19.494  14.575 1.00 30.77 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.668 18.305  15.175 1.00 30.66 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.508 17.369  14.754 1.00 27.45 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.868  18.047  16.206 1.00 29.74 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.522  20.075  12.623 1.00 33.52 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.245  18.772  12.034 1.00 33.06 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.570  18.054  11.793 1.00 28.77 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.436  18.578  11.100 1.00 28.63 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.481  18.862  10.715 1.00 35.70 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.057  19.349  10.849 1.00 40.51 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.005  18.459  11.032 1.00 43.63 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.758  20.698  10.768 1.00 43.59 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.683  18.907  11.098 1.00 46.60 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.453  21.156  10.842 1.00 45.92 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.420  20.263  11.019 1.00 48.51 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.851 20.790  11.062 1.00 53.23 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.732  16.846  12.350 1.00 25.35 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.928  16.066  12.066 1.00 21.73 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.596  15.171  10.871 1.00 20.18 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.539  14.521  10.867 1.00 21.15 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.389  15.265  13.284 1.00 21.47 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.519  14.287  12.978 1.00 19.61 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.208 13.830  14.240 1.00 17.18 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.413 14.612  15.184 1.00 16.66 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.581 12.543  14.287 1.00 13.16 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.404  15.222  9.813  1.00 17.35 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.148  14.387  8.629  1.00 16.89 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.858  13.018  8.745  1.00 17.17 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.670  12.808  9.658  1.00 16.34 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.582  15.113  7.357  1.00 17.68 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 9.962  15.428  7.428  1.00 19.10 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.476  12.072  7.862  1.00 17.87 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.053  10.735  7.772  1.00 17.95 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.910  9.961   9.093  1.00 17.50 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.787  9.172   9.460  1.00 15.52 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.502 10.828  7.265  1.00 19.79 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.621 11.500  5.919  1.00 25.08 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.548 10.770  4.739  1.00 28.39 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.741 12.811  5.606  1.00 26.91 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.656 11.656  3.755  1.00 28.93 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.755 12.894  4.226  1.00 28.86 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.781  10.180  9.782  1.00 18.02 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.513  9.590   11.091 1.00 18.31 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.447  8.502   11.007 1.00 18.01 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.438  8.669   10.330 1.00 17.74 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.035  10.732  12.015 1.00 18.83 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.985  10.451  13.522 1.00 20.52 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.352  10.018  14.046 1.00 20.09 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.515  11.720  14.280 1.00 22.06 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.659  7.417   11.740 1.00 17.12 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.761  6.248   11.742 1.00 18.07 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.338  5.968   13.163 1.00 18.17 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.213  5.816   13.991 1.00 17.88 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.541  5.028   11.233 1.00 18.92 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.107  5.246   9.841  1.00 21.44 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.160  3.941   9.213  1.00 22.22 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.581  4.058   10.265 1.00 16.55 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.034  5.856   13.457 1.00 18.35 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.589  5.584   14.824 1.00 19.42 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.167  4.136   14.991 1.00 19.09 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.695  3.502   14.043 1.00 20.01 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.372  6.484   15.219 1.00 21.38 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.667  7.984   15.323 1.00 25.22 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.465  8.710   15.834 1.00 27.13 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.788  8.260   16.289 1.00 25.58 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.284  3.660   16.210 1.00 18.95 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.862  2.331   16.642 1.00 19.54 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.306  2.463   18.056 1.00 20.03 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.635  3.402   18.776 1.00 20.24 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.061  1.397   16.656 1.00 20.02 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.479  1.517   18.465 1.00 20.15 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.981  1.463   19.833 1.00 21.44 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.031  0.667   20.609 1.00 22.91 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.387  -0.433  20.207 1.00 24.06 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.391 0.767   19.894 1.00 23.22 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.891 0.684   21.329 1.00 23.65 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.402 1.504   19.023 1.00 23.64 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.559  1.256   21.656 1.00 22.95 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.583  0.630   22.458 1.00 24.32 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.204  1.593   23.436 1.00 25.68 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.097  2.810   23.282 1.00 27.89 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.834  1.052   24.469 1.00 24.74 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.498  1.834   25.471 1.00 25.18 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.788  2.524   24.989 1.00 24.89 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.599  1.937   24.280 1.00 24.13 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.789  0.960   26.701 1.00 26.75 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.379  1.758   27.808 1.00 29.55 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.646  2.720   28.448 1.00 34.22 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.663  1.839   28.212 1.00 31.32 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.485  3.315   29.283 1.00 35.40 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.718  2.817   29.160 1.00 34.73 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.961  3.771   25.413 1.00 25.58 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.163  4.555   25.187 1.00 26.40 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.227  5.710   26.192 1.00 28.50 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.195  6.209   26.636 1.00 29.41 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.242  5.073   23.760 1.00 26.32 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.297  6.098   23.519 1.00 28.63 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.444  6.092   26.577 1.00 29.16 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.789  7.206   27.471 1.00 30.15 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.955 8.002   26.815 1.00 30.81 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.578 7.474   25.888 1.00 30.49 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.135 6.683   28.868 1.00 33.62 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 8.911  6.108   29.544 1.00 40.38 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.124  5.404   30.869 1.00 45.71 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 9.980  5.854   31.656 1.00 45.48 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.433  4.395   31.120 1.00 47.50 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.201 9.292   27.143 1.00 31.62 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.211 10.067  26.374 1.00 31.37 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.570 9.400   26.147 1.00 30.83 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.094 9.453   25.030 1.00 30.48 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.352 11.373  27.154 1.00 32.09 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.137 11.475  27.979 1.00 33.22 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.491 10.136  28.128 1.00 31.94 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.117 8.748   27.171 1.00 29.64 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.393 8.044   27.054 1.00 28.29 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.400 6.865   26.089 1.00 26.21 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.464 6.288   25.824 1.00 26.32 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.210 6.462   25.579 1.00 24.00 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.072 5.383   24.607 1.00 22.12 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.459 5.771   23.181 1.00 19.41 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.617 4.884   22.332 1.00 18.01 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.655 4.789   24.580 1.00 22.30 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.375 3.925   25.771 1.00 23.05 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.314 3.305   26.279 1.00 22.79 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.239 3.941   26.249 1.00 23.85 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.572 7.079   22.906 1.00 18.79 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.974 7.606   21.595 1.00 17.72 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.300 6.982   21.168 1.00 15.92 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.199 6.812   22.007 1.00 17.05 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.048 9.133   21.623 1.00 18.78 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.421 9.938   21.625 1.00 21.74 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.370 6.524   19.931 1.00 14.72 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.587 5.873   19.447 1.00 14.94 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.460 4.362   19.393 1.00 15.26 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.242 3.703   18.712 1.00 15.38 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.434 3.797   20.038 1.00 14.48 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.184 2.357   19.954 1.00 13.05 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.808 2.007   18.528 1.00 10.65 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.116 2.777   17.872 1.00 10.04 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.322 0.901   18.023 1.00 9.72  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.138 0.528   16.642 1.00 9.86  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.827 -0.225  16.437 1.00 9.18  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.428 -1.057  17.296 1.00 9.62  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.406 -0.307  16.212 1.00 13.06 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.582 0.622   15.780 1.00 16.06 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.115 -1.345  15.150 1.00 14.05 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.950 -0.144  15.692 1.00 16.86 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.196 0.045   15.291 1.00 8.28  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.016 -0.684  14.817 1.00 9.92  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.524 -1.516  13.624 1.00 10.93 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.194 -0.989  12.726 1.00 10.13 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 11.962 0.293   14.299 1.00 9.98  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.745 -0.363  13.568 1.00 11.88 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 9.934  -1.270  14.501 1.00 12.48 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.867  0.739   12.972 1.00 13.54 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.230 -2.821  13.613 1.00 12.47 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.727 -3.705  12.582 1.00 14.38 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.615 -4.533  12.000 1.00 14.80 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.811 -5.034  12.762 1.00 12.32 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.614 -4.739  13.262 1.00 17.96 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.023 -4.357  13.473 1.00 24.39 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 16.759 -5.577  14.008 1.00 29.17 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 18.199 -5.356  13.929 1.00 34.40 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.938 -5.569  12.844 1.00 35.19 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 18.395 -6.104  11.755 1.00 32.67 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 20.225 -5.274  12.849 1.00 36.52 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.694 -4.844  10.709 1.00 17.10 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.764 -5.799  10.078 1.00 20.37 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.636 -6.977  9.561  1.00 23.20 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.849 -7.010  9.835  1.00 23.08 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.005 -5.126  8.932  1.00 21.58 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.074 -4.518  7.616  1.00 22.56 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.047 -7.939  8.830  1.00 26.19 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 12.826 -9.062  8.286  1.00 29.55 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 13.936 -8.587  7.325  1.00 31.58 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 14.927 -9.303  7.130  1.00 32.97 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 11.897 -10.043 7.516  1.00 33.01 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.272 -9.410  6.274  1.00 38.60 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.141 -10.207 5.691  1.00 46.32 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 8.971  -10.031 6.064  1.00 49.01 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.465 -11.098 4.765  1.00 48.07 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.768 -7.404  6.705  1.00 31.30 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.726 -6.885  5.724  1.00 30.01 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 15.882 -6.074  6.344  1.00 27.90 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 16.786 -5.644  5.604  1.00 28.47 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.010 -5.992  4.696  1.00 31.85 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.844 -6.624  3.992  1.00 35.97 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.554 -6.376  4.390  1.00 38.72 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.807 -7.337  2.839  1.00 38.40 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.771 -7.021  3.540  1.00 40.16 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.480 -7.646  2.605  1.00 39.43 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.826 -5.804  7.664  1.00 24.25 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.882 -5.026  8.296  1.00 21.72 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.394 -3.839  9.128  1.00 18.85 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.249 -3.812  9.583  1.00 19.59 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.262 -2.866  9.345  1.00 17.61 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.966 -1.674  10.164 1.00 16.31 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.984 -0.767  9.447  1.00 15.17 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.282 -0.336  8.323  1.00 15.27 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.252 -0.880  10.536 1.00 16.90 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.883 0.423   11.234 1.00 17.12 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.154 -1.716  11.442 1.00 17.31 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.831 -0.455  10.086 1.00 13.04 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.779 0.410   9.524  1.00 13.11 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.920 1.913   9.950  1.00 12.44 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.770 2.840   9.140  1.00 13.90 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.353 -0.123  9.892  1.00 14.39 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.269 0.852   9.470  1.00 16.16 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.069 -1.496  9.309  1.00 15.16 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.178 2.118   11.228 1.00 10.55 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.265 3.468   11.769 1.00 10.26 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.652 3.491   13.231 1.00 9.64  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.076 2.478   13.774 1.00 7.94  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.522 4.644   13.871 1.00 10.10 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.873 4.754   15.291 1.00 10.40 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.805 5.482   16.064 1.00 9.28  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.163 6.390   15.534 1.00 8.87  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.213 5.466   15.483 1.00 12.18 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.253 6.817   14.781 1.00 13.94 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.413 4.590   15.106 1.00 12.99 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.460 7.588   15.237 1.00 14.65 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.601 5.114   17.341 1.00 9.18  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.621 5.830   18.171 1.00 9.18  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.943 7.337   18.218 1.00 9.90  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.101 7.684   18.389 1.00 10.35 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.536 5.266   19.596 1.00 10.29 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.501 6.053   20.383 1.00 10.16 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.130 3.802   19.539 1.00 11.57 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.934 8.207   18.014 1.00 11.12 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.139 9.652   17.989 1.00 12.25 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.119 10.406  18.840 1.00 16.21 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.431 11.502  19.354 1.00 17.71 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.110 10.159  16.548 1.00 13.02 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.217 11.575  16.519 1.00 16.04 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.883  9.886   18.916 1.00 18.69 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.794  10.514  19.714 1.00 21.73 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.996  9.457   20.481 1.00 24.77 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.130  8.281   20.207 1.00 23.56 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.832  11.376  18.836 1.00 24.01 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.207  10.583  17.833 1.00 25.46 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.480  12.554  18.225 1.00 25.21 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.146  9.880   21.416 1.00 27.81 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.289  8.958   22.141 1.00 30.42 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.407  9.657   23.151 1.00 32.29 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.480  10.873  23.328 1.00 32.14 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.573  8.881   23.793 1.00 34.78 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.651  9.383   24.802 1.00 38.49 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.262  8.814   24.614 1.00 41.50 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.865  8.522   23.488 1.00 41.54 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.520  8.640   25.715 1.00 43.17 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.133  8.178   25.687 1.00 43.91 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.078 6.805   25.076 1.00 41.80 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.142 6.543   24.518 1.00 43.01 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.745 9.222   24.982 1.00 47.31 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.804 10.504  25.741 1.00 53.15 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.832 10.488  26.974 1.00 56.07 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.824 11.638  25.034 1.00 54.01 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.876  5.906   25.271 1.00 38.38 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.774  4.560   24.733 1.00 35.94 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.157  4.460   23.270 1.00 32.75 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.913  3.434   22.631 1.00 33.48 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.808  5.489   22.742 1.00 30.20 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.251  5.495   21.365 1.00 27.84 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.770  5.609   21.309 1.00 26.25 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.372  6.272   22.150 1.00 27.91 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.634  6.696   20.625 1.00 27.14 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.097  6.753   20.606 1.00 30.78 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.383 8.133   20.247 1.00 32.14 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.462 5.701   19.658 1.00 32.42 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.373  5.069   20.245 1.00 22.23 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.783  5.225   20.007 1.00 18.97 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.972  5.649   18.544 1.00 16.95 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.336  5.089   17.661 1.00 16.70 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.609  3.967   20.397 1.00 18.61 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.108  2.706   19.688 1.00 18.33 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.087  4.200   20.129 1.00 18.47 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.789  6.663   18.318 1.00 15.45 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.061  7.199   16.983 1.00 14.93 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.475  6.920   16.535 1.00 15.07 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.411  7.083   17.321 1.00 15.34 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.652  6.465   15.261 1.00 13.33 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.983  6.103   14.751 1.00 10.76 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.331 6.988   13.528 1.00 9.99  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.494  7.206   12.637 1.00 9.57  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.002 4.621   14.303 1.00 9.79  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.464  3.628   15.307 1.00 10.60 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.283 3.090   16.287 1.00 10.82 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.161  3.164   15.219 1.00 10.49 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.784  2.199   17.226 1.00 9.85  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.673  2.238   16.147 1.00 10.76 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.494  1.776   17.153 1.00 10.07 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.575 7.495   13.503 1.00 9.42  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.064 8.262   12.370 1.00 10.07 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.491 7.250   11.306 1.00 10.71 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.395 6.469   11.542 1.00 10.25 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.265 9.099   12.789 1.00 9.92  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.843 7.248   10.145 1.00 12.23 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.184 6.313   9.060  1.00 13.59 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.546 6.614   8.464  1.00 14.98 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.891 7.789   8.358  1.00 14.79 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.154 6.478   7.948  1.00 16.62 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.285 5.413   6.871  1.00 22.52 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.423 4.241   7.227  1.00 21.94 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.325 5.780   5.662  1.00 23.54 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.310 5.570   8.060  1.00 14.61 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.607 5.747   7.381  1.00 15.69 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.655 4.962   6.058  1.00 17.88 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.657 5.028   5.366  1.00 19.15 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.844 5.408   8.234  1.00 14.71 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.848 6.201   9.547  1.00 15.33 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.940 3.899   8.495  1.00 13.53 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.592 4.242   5.698  1.00 17.78 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.569 3.420   4.511  1.00 18.59 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.679 4.191   3.206  1.00 22.01 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.137 3.616   2.206  1.00 23.33 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.313 2.558   4.502  1.00 17.54 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.218 1.648   5.704  1.00 17.12 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.913 0.882   5.621  1.00 17.29 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.799 1.737   6.058  1.00 19.70 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.540  1.332   6.144  1.00 21.63 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.216  0.085   5.825  1.00 21.93 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.601  2.152   6.615  1.00 19.88 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.262 5.463   3.192  1.00 23.15 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.369 6.260   1.958  1.00 25.13 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.770 6.828   1.703  1.00 26.52 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.023 7.391   0.605  1.00 27.05 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.367 7.425   1.962  1.00 26.51 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.645 8.464   3.023  1.00 29.38 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.943 8.066   4.179  1.00 28.45 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.535 9.671   2.710  1.00 29.08 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.660 6.793   2.705  1.00 26.36 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.007 7.395   2.526  1.00 26.46 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 18.910 6.405   1.817  1.00 29.06 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.700 5.724   2.467  1.00 29.24 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.592 7.799   3.886  1.00 24.98 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.691 8.718   4.720  1.00 24.91 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.266 8.960   6.094  1.00 24.38 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.398 9.993   4.006  1.00 25.89 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.738 6.264   0.492  1.00 30.82 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.451 5.250   -0.309 1.00 33.00 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 20.977 5.426   -0.347 1.00 34.74 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.721 4.449   -0.514 1.00 36.30 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.892 5.175   -1.737 1.00 34.05 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.394 5.045   -1.932 1.00 35.58 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.059 5.016   -3.433 1.00 37.32 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.840 3.821   -1.190 1.00 36.75 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.432 6.658   -0.134 1.00 34.34 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.836 7.020   -0.095 1.00 34.17 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.605 6.442   1.092  1.00 36.20 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.839 6.445   1.062  1.00 37.30 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.008 8.544   -0.162 1.00 32.26 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.296 9.320   0.921  1.00 30.00 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.057 9.883   0.848  1.00 29.52 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.818 9.668   2.214  1.00 28.81 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.780 10.569  2.011  1.00 29.24 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.846 10.455  2.862  1.00 28.79 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.042 9.450   2.857  1.00 29.30 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.037 10.976  4.137  1.00 29.32 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.232 9.971   4.121  1.00 30.15 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.240 10.739  4.744  1.00 30.00 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.910 5.971   2.145  1.00 36.78 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.601 5.361   3.277  1.00 38.26 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.383 4.101   2.845  1.00 43.01 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.283 3.696   3.563  1.00 43.29 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.588 4.976   4.373  1.00 36.53 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.961 6.129   5.146  1.00 35.65 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.820 5.629   6.032  1.00 35.60 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.000 6.839   6.006  1.00 35.88 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.032 3.483   1.688  1.00 46.85 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.645 2.257   1.158  1.00 51.08 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.690 2.417   0.068  1.00 55.85 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.276 1.403   -0.313 1.00 57.57 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.559 1.385   0.552  1.00 53.68 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.665 0.783   1.582  1.00 57.70 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.174 0.407   2.652  1.00 58.64 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.451 0.691   1.323  1.00 60.59 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.836 3.606   -0.532 1.00 57.73 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.786 3.783   -1.639 1.00 60.62 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.845 4.843   -1.357 1.00 62.81 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.677 5.136   -2.228 1.00 64.49 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.046 4.110   -2.948 1.00 63.77 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.249 5.404   -2.887 1.00 70.21 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 23.878 5.345   -3.534 1.00 77.29 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.304 6.425   -3.811 1.00 78.75 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.375 4.220   -3.760 1.00 79.51 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BRE B 2 .   ? 9.881  14.717  22.442 1.00 31.75 ? 201 A1BRE A N1  1 
HETATM 1079 C  C4  . A1BRE B 2 .   ? 8.368  11.359  25.302 1.00 33.99 ? 201 A1BRE A C4  1 
HETATM 1080 C  C5  . A1BRE B 2 .   ? 9.296  11.672  24.320 1.00 33.62 ? 201 A1BRE A C5  1 
HETATM 1081 C  C6  . A1BRE B 2 .   ? 9.380  13.476  22.726 1.00 31.96 ? 201 A1BRE A C6  1 
HETATM 1082 C  C7  . A1BRE B 2 .   ? 11.037 15.287  23.152 1.00 31.59 ? 201 A1BRE A C7  1 
HETATM 1083 C  C8  . A1BRE B 2 .   ? 12.329 14.861  22.476 1.00 30.51 ? 201 A1BRE A C8  1 
HETATM 1084 C  C10 . A1BRE B 2 .   ? 11.036 14.636  20.292 1.00 28.92 ? 201 A1BRE A C10 1 
HETATM 1085 C  C13 . A1BRE B 2 .   ? 9.884  10.660  23.566 1.00 33.13 ? 201 A1BRE A C13 1 
HETATM 1086 O  O1  . A1BRE B 2 .   ? 10.677 16.271  18.572 1.00 27.98 ? 201 A1BRE A O1  1 
HETATM 1087 C  C11 . A1BRE B 2 .   ? 10.960 15.102  18.849 1.00 27.85 ? 201 A1BRE A C11 1 
HETATM 1088 N  N2  . A1BRE B 2 .   ? 11.245 14.193  17.931 1.00 26.25 ? 201 A1BRE A N2  1 
HETATM 1089 C  C9  . A1BRE B 2 .   ? 12.293 15.187  20.980 1.00 29.56 ? 201 A1BRE A C9  1 
HETATM 1090 C  C12 . A1BRE B 2 .   ? 9.820  15.172  21.051 1.00 30.80 ? 201 A1BRE A C12 1 
HETATM 1091 O  O   . A1BRE B 2 .   ? 8.624  12.889  21.961 1.00 31.20 ? 201 A1BRE A O   1 
HETATM 1092 N  N   . A1BRE B 2 .   ? 9.657  12.983  23.953 1.00 33.19 ? 201 A1BRE A N   1 
HETATM 1093 C  C3  . A1BRE B 2 .   ? 8.000  10.040  25.492 1.00 34.14 ? 201 A1BRE A C3  1 
HETATM 1094 C  C2  . A1BRE B 2 .   ? 8.575  9.039   24.720 1.00 33.00 ? 201 A1BRE A C2  1 
HETATM 1095 C  C1  . A1BRE B 2 .   ? 9.535  9.333   23.760 1.00 32.40 ? 201 A1BRE A C1  1 
HETATM 1096 C  C   . A1BRE B 2 .   ? 10.181 8.239   22.944 1.00 31.75 ? 201 A1BRE A C   1 
HETATM 1097 ZN ZN  . ZN    C 3 .   ? 10.777 -4.649  5.552  1.00 25.85 2 202 ZN    A ZN  1 
HETATM 1098 S  S   . DMS   D 4 .   ? 19.557 -0.382  19.986 1.00 63.10 ? 203 DMS   A S   1 
HETATM 1099 O  O   . DMS   D 4 .   ? 18.109 -0.606  19.668 1.00 62.42 ? 203 DMS   A O   1 
HETATM 1100 C  C1  . DMS   D 4 .   ? 19.768 0.315   21.643 1.00 63.10 ? 203 DMS   A C1  1 
HETATM 1101 C  C2  . DMS   D 4 .   ? 20.194 1.097   19.135 1.00 63.16 ? 203 DMS   A C2  1 
HETATM 1102 S  S   . DMS   E 4 .   ? 3.460  11.292  18.776 1.00 86.06 ? 204 DMS   A S   1 
HETATM 1103 O  O   . DMS   E 4 .   ? 4.015  12.615  19.220 1.00 85.92 ? 204 DMS   A O   1 
HETATM 1104 C  C1  . DMS   E 4 .   ? 1.796  11.591  18.104 1.00 86.06 ? 204 DMS   A C1  1 
HETATM 1105 C  C2  . DMS   E 4 .   ? 2.908  10.410  20.264 1.00 86.00 ? 204 DMS   A C2  1 
HETATM 1106 O  O   . HOH   F 5 .   ? 34.426 16.124  20.274 1.00 29.79 ? 301 HOH   A O   1 
HETATM 1107 O  O   . HOH   F 5 .   ? 9.021  2.181   2.907  1.00 26.79 ? 302 HOH   A O   1 
HETATM 1108 O  O   . HOH   F 5 .   ? 3.021  7.837   9.754  1.00 31.33 ? 303 HOH   A O   1 
HETATM 1109 O  O   . HOH   F 5 .   ? 22.679 -4.830  12.047 1.00 40.07 ? 304 HOH   A O   1 
HETATM 1110 O  O   . HOH   F 5 .   ? 7.693  -3.974  0.694  1.00 21.62 ? 305 HOH   A O   1 
HETATM 1111 O  O   . HOH   F 5 .   ? 3.977  -4.932  21.219 1.00 32.69 ? 306 HOH   A O   1 
HETATM 1112 O  O   . HOH   F 5 .   ? 23.099 18.146  19.574 1.00 40.23 ? 307 HOH   A O   1 
HETATM 1113 O  O   . HOH   F 5 .   ? 23.557 0.011   15.511 1.00 46.79 ? 308 HOH   A O   1 
HETATM 1114 O  O   . HOH   F 5 .   ? 12.183 7.063   31.251 1.00 34.08 ? 309 HOH   A O   1 
HETATM 1115 O  O   . HOH   F 5 .   ? 6.968  3.202   32.837 1.00 27.95 ? 310 HOH   A O   1 
HETATM 1116 O  O   . HOH   F 5 .   ? 20.029 8.709   19.018 1.00 19.58 ? 311 HOH   A O   1 
HETATM 1117 O  O   . HOH   F 5 .   ? 10.573 8.048   4.686  1.00 44.14 ? 312 HOH   A O   1 
HETATM 1118 O  O   . HOH   F 5 .   ? 8.407  19.777  18.088 1.00 28.10 ? 313 HOH   A O   1 
HETATM 1119 O  O   . HOH   F 5 .   ? 10.874 -5.262  31.772 1.00 31.56 ? 314 HOH   A O   1 
HETATM 1120 O  O   . HOH   F 5 .   ? 1.156  -2.786  20.273 1.00 34.57 ? 315 HOH   A O   1 
HETATM 1121 O  O   . HOH   F 5 .   ? 20.496 18.873  21.411 1.00 40.33 ? 316 HOH   A O   1 
HETATM 1122 O  O   . HOH   F 5 .   ? 14.811 2.361   23.190 1.00 16.67 ? 317 HOH   A O   1 
HETATM 1123 O  O   . HOH   F 5 .   ? 9.872  4.233   33.794 1.00 40.64 ? 318 HOH   A O   1 
HETATM 1124 O  O   . HOH   F 5 .   ? 10.169 4.789   3.437  1.00 24.98 ? 319 HOH   A O   1 
HETATM 1125 O  O   . HOH   F 5 .   ? -0.706 -4.967  15.694 0.50 22.93 ? 320 HOH   A O   1 
HETATM 1126 O  O   . HOH   F 5 .   ? 17.690 2.486   23.177 1.00 24.07 ? 321 HOH   A O   1 
HETATM 1127 O  O   . HOH   F 5 .   ? 11.058 2.014   33.508 1.00 24.14 ? 322 HOH   A O   1 
HETATM 1128 O  O   . HOH   F 5 .   ? 10.837 -9.044  24.635 1.00 28.58 ? 323 HOH   A O   1 
HETATM 1129 O  O   . HOH   F 5 .   ? 0.388  -0.363  16.539 1.00 18.89 ? 324 HOH   A O   1 
HETATM 1130 O  O   . HOH   F 5 .   ? 11.302 11.477  11.482 1.00 14.25 ? 325 HOH   A O   1 
HETATM 1131 O  O   . HOH   F 5 .   ? 17.631 21.037  9.569  1.00 19.05 ? 326 HOH   A O   1 
HETATM 1132 O  O   . HOH   F 5 .   ? 30.038 11.038  19.229 1.00 28.55 ? 327 HOH   A O   1 
HETATM 1133 O  O   . HOH   F 5 .   ? 17.888 18.785  17.047 1.00 19.82 ? 328 HOH   A O   1 
HETATM 1134 O  O   . HOH   F 5 .   ? 5.334  -1.734  24.363 1.00 22.85 ? 329 HOH   A O   1 
HETATM 1135 O  O   . HOH   F 5 .   ? 16.002 13.587  26.281 1.00 38.60 ? 330 HOH   A O   1 
HETATM 1136 O  O   . HOH   F 5 .   ? 13.104 10.311  9.420  1.00 10.65 ? 331 HOH   A O   1 
HETATM 1137 O  O   . HOH   F 5 .   ? 18.749 9.040   25.612 1.00 33.99 ? 332 HOH   A O   1 
HETATM 1138 O  O   . HOH   F 5 .   ? 15.171 11.975  24.161 1.00 23.92 ? 333 HOH   A O   1 
HETATM 1139 O  O   . HOH   F 5 .   ? 13.254 9.098   29.899 1.00 36.84 ? 334 HOH   A O   1 
HETATM 1140 O  O   . HOH   F 5 .   ? 4.106  -5.352  6.592  1.00 27.52 ? 335 HOH   A O   1 
HETATM 1141 O  O   . HOH   F 5 .   ? 14.202 20.772  8.042  1.00 32.18 ? 336 HOH   A O   1 
HETATM 1142 O  O   . HOH   F 5 .   ? 0.573  1.206   24.451 1.00 37.67 ? 337 HOH   A O   1 
HETATM 1143 O  O   . HOH   F 5 .   ? 22.229 18.740  5.949  1.00 23.81 ? 338 HOH   A O   1 
HETATM 1144 O  O   . HOH   F 5 .   ? 4.314  5.562   24.996 1.00 28.03 ? 339 HOH   A O   1 
HETATM 1145 O  O   . HOH   F 5 .   ? 24.584 7.287   20.407 1.00 37.98 ? 340 HOH   A O   1 
HETATM 1146 O  O   . HOH   F 5 .   ? 21.517 -5.621  10.215 1.00 30.69 ? 341 HOH   A O   1 
HETATM 1147 O  O   . HOH   F 5 .   ? 21.272 19.194  17.759 1.00 27.25 ? 342 HOH   A O   1 
HETATM 1148 O  O   . HOH   F 5 .   ? 5.613  1.574   6.858  1.00 29.97 ? 343 HOH   A O   1 
HETATM 1149 O  O   . HOH   F 5 .   ? 18.170 19.143  5.205  1.00 38.34 ? 344 HOH   A O   1 
HETATM 1150 O  O   . HOH   F 5 .   ? 8.323  -7.569  8.819  1.00 39.74 ? 345 HOH   A O   1 
HETATM 1151 O  O   . HOH   F 5 .   ? 14.734 -4.719  17.261 1.00 19.79 ? 346 HOH   A O   1 
HETATM 1152 O  O   . HOH   F 5 .   ? 5.200  7.594   28.491 1.00 42.87 ? 347 HOH   A O   1 
HETATM 1153 O  O   . HOH   F 5 .   ? 15.837 -4.714  1.716  1.00 32.80 ? 348 HOH   A O   1 
HETATM 1154 O  O   . HOH   F 5 .   ? 22.025 8.587   20.966 1.00 25.02 ? 349 HOH   A O   1 
HETATM 1155 O  O   . HOH   F 5 .   ? 2.697  3.381   27.629 1.00 31.81 ? 350 HOH   A O   1 
HETATM 1156 O  O   . HOH   F 5 .   ? 19.828 23.405  15.706 1.00 24.37 ? 351 HOH   A O   1 
HETATM 1157 O  O   . HOH   F 5 .   ? 18.237 0.367   30.202 1.00 29.62 ? 352 HOH   A O   1 
HETATM 1158 O  O   . HOH   F 5 .   ? 1.470  -2.626  17.592 1.00 25.06 ? 353 HOH   A O   1 
HETATM 1159 O  O   . HOH   F 5 .   ? 11.876 21.305  12.274 1.00 31.53 ? 354 HOH   A O   1 
HETATM 1160 O  O   . HOH   F 5 .   ? 24.036 2.179   19.440 1.00 43.24 ? 355 HOH   A O   1 
HETATM 1161 O  O   . HOH   F 5 .   ? 3.507  -2.853  22.263 1.00 52.38 ? 356 HOH   A O   1 
HETATM 1162 O  O   . HOH   F 5 .   ? 18.140 -7.861  16.247 1.00 38.36 ? 357 HOH   A O   1 
HETATM 1163 O  O   . HOH   F 5 .   ? 31.602 8.861   5.210  1.00 39.00 ? 358 HOH   A O   1 
HETATM 1164 O  O   . HOH   F 5 .   ? 6.352  23.118  11.221 1.00 43.96 ? 359 HOH   A O   1 
HETATM 1165 O  O   . HOH   F 5 .   ? 0.217  -2.959  9.591  1.00 36.97 ? 360 HOH   A O   1 
HETATM 1166 O  O   . HOH   F 5 .   ? 22.147 15.985  23.928 1.00 42.39 ? 361 HOH   A O   1 
HETATM 1167 O  O   . HOH   F 5 .   ? 19.587 8.663   -2.413 1.00 35.26 ? 362 HOH   A O   1 
HETATM 1168 O  O   . HOH   F 5 .   ? 7.086  11.604  4.371  1.00 29.30 ? 363 HOH   A O   1 
HETATM 1169 O  O   . HOH   F 5 .   ? 20.674 21.777  17.822 1.00 23.02 ? 364 HOH   A O   1 
HETATM 1170 O  O   . HOH   F 5 .   ? 16.935 -3.699  18.122 1.00 46.06 ? 365 HOH   A O   1 
HETATM 1171 O  O   . HOH   F 5 .   ? 18.023 12.986  2.070  1.00 41.64 ? 366 HOH   A O   1 
HETATM 1172 O  O   . HOH   F 5 .   ? 15.271 -9.628  12.032 1.00 32.21 ? 367 HOH   A O   1 
HETATM 1173 O  O   . HOH   F 5 .   ? 28.695 16.550  23.758 1.00 53.95 ? 368 HOH   A O   1 
HETATM 1174 O  O   . HOH   F 5 .   ? 7.443  13.793  2.709  1.00 40.47 ? 369 HOH   A O   1 
HETATM 1175 O  O   . HOH   F 5 .   ? 1.938  1.108   26.886 1.00 36.83 ? 370 HOH   A O   1 
HETATM 1176 O  O   . HOH   F 5 .   ? 8.625  19.311  7.042  1.00 50.04 ? 371 HOH   A O   1 
HETATM 1177 O  O   . HOH   F 5 .   ? 35.506 15.878  16.325 0.50 70.15 ? 372 HOH   A O   1 
HETATM 1178 O  O   . HOH   F 5 .   ? 9.235  7.133   2.466  1.00 33.24 ? 373 HOH   A O   1 
HETATM 1179 O  O   . HOH   F 5 .   ? 11.874 23.319  13.967 1.00 31.10 ? 374 HOH   A O   1 
HETATM 1180 O  O   . HOH   F 5 .   ? 26.246 -7.758  5.908  1.00 44.31 ? 375 HOH   A O   1 
HETATM 1181 O  O   . HOH   F 5 .   ? -2.373 -2.203  8.986  1.00 26.72 ? 376 HOH   A O   1 
HETATM 1182 O  O   . HOH   F 5 .   ? 22.732 9.803   23.390 1.00 39.49 ? 377 HOH   A O   1 
HETATM 1183 O  O   . HOH   F 5 .   ? 20.029 -3.794  22.343 1.00 50.06 ? 378 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 1   ? 0.6699 0.2465 0.3072 -0.1101 -0.2150 0.0328  7   SER   A N   
2    C CA  . SER   A 1   ? 0.6205 0.2452 0.3573 -0.1042 -0.2377 0.0482  7   SER   A CA  
3    C C   . SER   A 1   ? 0.5362 0.2310 0.3742 -0.0828 -0.2208 0.0522  7   SER   A C   
4    O O   . SER   A 1   ? 0.5356 0.2388 0.3655 -0.0785 -0.2069 0.0487  7   SER   A O   
5    C CB  . SER   A 1   ? 0.6624 0.2477 0.3966 -0.1374 -0.3000 0.0782  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.7006 0.2794 0.4409 -0.1519 -0.3249 0.0971  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.4650 0.2016 0.3924 -0.0719 -0.2190 0.0590  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.4001 0.1875 0.4171 -0.0561 -0.1956 0.0613  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3602 0.1808 0.4275 -0.0401 -0.1658 0.0512  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3559 0.1725 0.3833 -0.0349 -0.1551 0.0369  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3112 0.1585 0.4662 -0.0341 -0.1495 0.0596  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2910 0.1589 0.4872 -0.0234 -0.1160 0.0500  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2727 0.1561 0.5140 -0.0180 -0.0738 0.0441  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2677 0.1512 0.5357 -0.0208 -0.0759 0.0537  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2659 0.1306 0.5334 -0.0272 -0.1366 0.0711  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2631 0.1521 0.5094 -0.0139 -0.0352 0.0296  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2577 0.1431 0.5338 -0.0152 0.0125  0.0217  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2659 0.1434 0.6319 -0.0133 0.0333  0.0342  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2526 0.1309 0.6195 -0.0114 0.0268  0.0343  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2708 0.1533 0.4699 -0.0205 0.0402  -0.0019 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2860 0.1796 0.4123 -0.0205 0.0192  -0.0088 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2752 0.1361 0.4821 -0.0299 0.0908  -0.0119 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.3071 0.2027 0.3746 -0.0278 0.0309  -0.0205 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2748 0.1438 0.7237 -0.0132 0.0612  0.0464  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2711 0.1289 0.8250 -0.0102 0.0914  0.0622  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3148 0.1402 0.8636 -0.0153 0.1671  0.0420  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3281 0.1429 0.8962 -0.0178 0.1928  0.0415  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2298 0.0972 0.9071 -0.0083 0.0660  0.1012  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2319 0.1150 0.9011 -0.0127 -0.0113 0.1236  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2336 0.1188 0.9515 -0.0135 -0.0387 0.1433  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2671 0.1541 0.8607 -0.0191 -0.0540 0.1214  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2558 0.1415 0.9397 -0.0239 -0.1087 0.1598  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2951 0.1781 0.8504 -0.0293 -0.1184 0.1363  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2953 0.1751 0.8941 -0.0335 -0.1470 0.1560  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3431 0.2063 0.8934 -0.0499 -0.2105 0.1710  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3527 0.1552 0.8633 -0.0204 0.2031  0.0246  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.4044 0.1570 0.8851 -0.0336 0.2783  0.0033  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.4148 0.1391 0.9603 -0.0321 0.3240  0.0084  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.4267 0.1622 0.9497 -0.0302 0.3018  0.0077  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.4734 0.2105 0.8058 -0.0521 0.2793  -0.0258 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.4853 0.2488 0.7605 -0.0508 0.2337  -0.0280 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.5262 0.1951 0.8065 -0.0752 0.3541  -0.0473 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.4098 0.0980 1.0498 -0.0311 0.3893  0.0168  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.4050 0.0623 1.1273 -0.0277 0.4416  0.0256  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3735 0.0810 1.1964 -0.0103 0.3820  0.0589  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3450 0.0961 1.2394 -0.0011 0.3231  0.0877  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3799 0.0802 1.1885 -0.0102 0.3872  0.0545  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3350 0.0785 1.2263 0.0029  0.3273  0.0848  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3211 0.1021 1.1008 0.0014  0.2501  0.0735  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3051 0.1055 1.1066 0.0067  0.2136  0.0854  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3699 0.0859 1.3311 0.0065  0.3774  0.0915  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4282 0.1163 1.5545 0.0138  0.4443  0.1186  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4092 0.1167 1.6452 0.0200  0.4301  0.1488  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4819 0.1213 1.6378 0.0126  0.5210  0.1117  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3218 0.1113 0.9909 -0.0056 0.2272  0.0528  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3211 0.1398 0.8914 -0.0064 0.1663  0.0425  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2741 0.1200 0.8331 -0.0042 0.1100  0.0530  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2588 0.1011 0.8366 -0.0057 0.1212  0.0561  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3671 0.1678 0.8056 -0.0199 0.1892  0.0101  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3891 0.1543 0.8057 -0.0294 0.2384  -0.0023 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3892 0.1659 0.8315 -0.0226 0.2225  0.0053  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.4370 0.1504 0.7890 -0.0495 0.2986  -0.0230 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.4295 0.1704 0.8459 -0.0328 0.2679  -0.0058 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4825 0.1506 0.7959 -0.0643 0.3447  -0.0349 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4864 0.1705 0.8344 -0.0549 0.3294  -0.0260 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.5544 0.1909 0.8598 -0.0709 0.3752  -0.0372 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2504 0.1168 0.7698 -0.0024 0.0531  0.0570  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2303 0.1096 0.7074 -0.0044 0.0022  0.0620  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2331 0.1175 0.5965 -0.0053 -0.0091 0.0382  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2425 0.1288 0.5884 -0.0035 -0.0146 0.0341  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2131 0.0964 0.7514 -0.0073 -0.0535 0.0938  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2542 0.1335 0.7120 -0.0154 -0.1085 0.0944  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2694 0.1393 0.7841 -0.0281 -0.1659 0.1307  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3353 0.1843 0.7575 -0.0396 -0.2108 0.1263  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3907 0.2154 0.7387 -0.0545 -0.2464 0.1285  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3633 0.1903 0.7217 -0.0580 -0.2473 0.1358  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4308 0.2223 0.6874 -0.0675 -0.2762 0.1218  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2202 0.1072 0.5164 -0.0077 -0.0092 0.0251  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2229 0.1162 0.4315 -0.0082 -0.0164 0.0091  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2274 0.1187 0.4004 -0.0075 -0.0546 0.0140  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2363 0.1244 0.4110 -0.0098 -0.0619 0.0188  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2255 0.1183 0.3859 -0.0149 0.0142  -0.0061 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2342 0.1374 0.3283 -0.0167 0.0049  -0.0137 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2188 0.0927 0.4004 -0.0234 0.0595  -0.0123 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2209 0.1072 0.3563 -0.0062 -0.0746 0.0121  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2439 0.1102 0.3282 -0.0099 -0.1022 0.0139  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2372 0.1018 0.2626 -0.0052 -0.0910 0.0010  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2279 0.1083 0.2620 -0.0007 -0.0764 -0.0033 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2733 0.1145 0.3713 -0.0194 -0.1411 0.0299  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2905 0.1261 0.4402 -0.0289 -0.1654 0.0517  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2648 0.1133 0.4004 -0.0158 -0.1406 0.0327  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2372 0.0763 0.2060 -0.0079 -0.0974 -0.0022 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2512 0.0788 0.1781 -0.0031 -0.0823 -0.0101 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2789 0.0925 0.2095 -0.0049 -0.0938 -0.0090 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.3083 0.0947 0.2344 -0.0160 -0.1221 -0.0020 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2778 0.0605 0.1399 -0.0092 -0.0820 -0.0137 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3173 0.1129 0.1753 -0.0065 -0.0697 -0.0144 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3423 0.1332 0.2025 -0.0136 -0.0865 -0.0095 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2872 0.1020 0.1495 0.0031  -0.0425 -0.0165 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2610 0.0932 0.2050 0.0033  -0.0766 -0.0119 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2582 0.0784 0.2078 0.0027  -0.0854 -0.0113 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3326 0.0934 0.2206 -0.0077 -0.0956 -0.0150 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3467 0.0846 0.2324 -0.0176 -0.1209 -0.0105 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2363 0.0864 0.2104 0.0121  -0.0643 -0.0113 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2250 0.0736 0.2185 0.0131  -0.0718 -0.0099 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1948 0.0659 0.2043 0.0205  -0.0509 -0.0069 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1906 0.0674 0.2239 0.0228  -0.0542 -0.0046 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2599 0.1058 0.2756 0.0239  -0.0524 -0.0080 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3029 0.1004 0.2674 0.0199  -0.0455 -0.0153 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2277 0.0838 0.2703 0.0268  -0.0541 -0.0050 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3608 0.0885 0.1948 -0.0092 -0.0756 -0.0219 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.4453 0.0966 0.1985 -0.0249 -0.0761 -0.0287 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.5105 0.1176 0.2195 -0.0499 -0.1194 -0.0217 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.5670 0.1033 0.2034 -0.0728 -0.1353 -0.0234 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.4765 0.0973 0.1890 -0.0196 -0.0320 -0.0374 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.4780 0.0942 0.1684 -0.0222 -0.0288 -0.0372 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.4518 0.1318 0.2019 -0.0069 -0.0203 -0.0313 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.5235 0.0720 0.1313 -0.0408 -0.0307 -0.0421 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.4758 0.1322 0.1879 -0.0131 -0.0181 -0.0328 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.5289 0.1069 0.1553 -0.0332 -0.0235 -0.0391 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.4919 0.1376 0.2480 -0.0491 -0.1414 -0.0106 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.5196 0.1343 0.2597 -0.0730 -0.1876 0.0049  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.5058 0.1558 0.3327 -0.0744 -0.2223 0.0247  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.5120 0.1482 0.3565 -0.0933 -0.2642 0.0464  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.5086 0.1350 0.2490 -0.0727 -0.1860 0.0081  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.5608 0.1423 0.2157 -0.0754 -0.1551 -0.0069 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.5514 0.1510 0.2160 -0.0739 -0.1557 -0.0023 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.6305 0.1132 0.1711 -0.1072 -0.1694 -0.0098 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.4777 0.1728 0.3670 -0.0555 -0.2042 0.0211  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.4515 0.1770 0.4306 -0.0548 -0.2265 0.0398  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.4912 0.1704 0.4550 -0.0806 -0.2767 0.0589  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.5396 0.1667 0.4193 -0.0942 -0.2818 0.0490  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.4249 0.1936 0.4528 -0.0339 -0.1949 0.0303  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.4774 0.1701 0.5241 -0.0900 -0.3126 0.0886  24  THR   A N   
135  C CA  . THR   A 18  ? 0.5215 0.1731 0.5711 -0.1201 -0.3725 0.1174  24  THR   A CA  
136  C C   . THR   A 18  ? 0.5079 0.1785 0.6221 -0.1124 -0.3756 0.1244  24  THR   A C   
137  O O   . THR   A 18  ? 0.4743 0.1893 0.6296 -0.0841 -0.3299 0.1067  24  THR   A O   
138  C CB  . THR   A 18  ? 0.5194 0.1815 0.6508 -0.1344 -0.4122 0.1553  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4773 0.2009 0.7461 -0.1094 -0.3861 0.1663  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.5465 0.1966 0.6275 -0.1401 -0.4086 0.1504  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.5361 0.1718 0.6623 -0.1406 -0.4328 0.1537  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.5304 0.1860 0.7307 -0.1337 -0.4385 0.1648  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.4569 0.1788 0.8095 -0.1079 -0.4128 0.1813  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4272 0.1813 0.8276 -0.0852 -0.3765 0.1698  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.5906 0.1934 0.7817 -0.1746 -0.5135 0.2008  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.7499 0.2723 0.7826 -0.2031 -0.5293 0.1808  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.8161 0.3325 0.7873 -0.1847 -0.4823 0.1433  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.8498 0.2883 0.7756 -0.2514 -0.5845 0.1954  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.9070 0.3347 0.7402 -0.2195 -0.5026 0.1338  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.9383 0.3114 0.7293 -0.2627 -0.5642 0.1629  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.4285 0.1642 0.8535 -0.1131 -0.4272 0.2080  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3727 0.1580 0.9440 -0.0918 -0.3945 0.2254  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3310 0.1487 0.8840 -0.0598 -0.3177 0.1843  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3055 0.1481 0.9350 -0.0422 -0.2795 0.1833  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4023 0.1906 1.0337 -0.1031 -0.4160 0.2557  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.5351 0.2822 1.1520 -0.1439 -0.5000 0.2971  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.6039 0.3091 1.1512 -0.1695 -0.5478 0.3035  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5486 0.3010 1.2279 -0.1551 -0.5222 0.3287  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3341 0.1462 0.7838 -0.0556 -0.2961 0.1529  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.2982 0.1351 0.7144 -0.0329 -0.2342 0.1175  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2847 0.1297 0.6879 -0.0223 -0.2136 0.1017  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2570 0.1243 0.6988 -0.0082 -0.1693 0.0922  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3249 0.1488 0.6299 -0.0346 -0.2277 0.0929  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3467 0.1709 0.6644 -0.0399 -0.2325 0.1023  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3112 0.1583 0.7152 -0.0319 -0.2089 0.1125  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3854 0.1814 0.6251 -0.0531 -0.2562 0.0995  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3098 0.1298 0.6527 -0.0319 -0.2434 0.0986  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3074 0.1355 0.6397 -0.0219 -0.2254 0.0849  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2972 0.1412 0.7320 -0.0171 -0.2246 0.1043  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2912 0.1528 0.7375 -0.0042 -0.1917 0.0920  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3376 0.1272 0.5800 -0.0342 -0.2509 0.0760  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3427 0.1249 0.4954 -0.0282 -0.2227 0.0493  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3857 0.1342 0.4633 -0.0396 -0.2305 0.0430  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3097 0.1182 0.4489 -0.0110 -0.1820 0.0303  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3967 0.1490 0.4227 -0.0279 -0.1934 0.0212  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3499 0.1414 0.4168 -0.0111 -0.1668 0.0157  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2755 0.1173 0.4584 0.0019  -0.1579 0.0274  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3284 0.1398 0.3802 0.0015  -0.1327 0.0033  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2756 0.1336 0.4294 0.0110  -0.1293 0.0142  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2960 0.1423 0.3931 0.0112  -0.1181 0.0046  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2949 0.1304 0.8078 -0.0297 -0.2627 0.1385  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2901 0.1394 0.9242 -0.0256 -0.2630 0.1652  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2797 0.1538 1.0023 -0.0080 -0.2031 0.1653  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2682 0.1508 1.0877 -0.0002 -0.1820 0.1806  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2716 0.1027 0.9724 -0.0489 -0.3286 0.2102  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2716 0.1497 0.9633 -0.0044 -0.1748 0.1505  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2402 0.1266 0.9864 0.0070  -0.1122 0.1445  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2345 0.1223 0.8711 0.0119  -0.0710 0.1048  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2226 0.1071 0.8586 0.0132  -0.0316 0.0954  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2512 0.1369 1.0670 0.0017  -0.1217 0.1691  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2762 0.1635 1.2364 -0.0038 -0.1519 0.2175  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2669 0.1570 1.3237 0.0052  -0.1194 0.2304  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2864 0.1691 1.2695 -0.0210 -0.2133 0.2488  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2356 0.1258 0.7839 0.0122  -0.0824 0.0850  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2329 0.1272 0.6879 0.0134  -0.0556 0.0565  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2370 0.1255 0.6982 0.0135  0.0026  0.0448  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2449 0.1275 0.7545 0.0159  0.0242  0.0500  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2200 0.1183 0.6183 0.0147  -0.0756 0.0473  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2176 0.1244 0.5353 0.0145  -0.0559 0.0267  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2373 0.1430 0.5000 0.0120  -0.0656 0.0198  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1996 0.1113 0.4903 0.0175  -0.0685 0.0233  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2245 0.1080 0.6260 0.0073  0.0276  0.0286  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2278 0.0910 0.5946 -0.0028 0.0789  0.0142  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2452 0.1176 0.5172 -0.0115 0.0676  0.0014  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2724 0.1359 0.5177 -0.0198 0.0835  -0.0026 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2568 0.1010 0.6234 -0.0095 0.1110  0.0093  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3093 0.1201 0.5997 -0.0292 0.1573  -0.0090 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2328 0.0663 0.7126 -0.0018 0.1316  0.0271  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2204 0.1101 0.4497 -0.0101 0.0388  -0.0008 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2131 0.1147 0.3771 -0.0174 0.0276  -0.0050 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1923 0.1113 0.3398 -0.0083 -0.0036 -0.0031 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1860 0.1016 0.3427 -0.0044 -0.0105 -0.0030 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2275 0.1095 0.3368 -0.0390 0.0550  -0.0120 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2294 0.1252 0.2822 -0.0508 0.0368  -0.0084 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2502 0.1500 0.2719 -0.0653 0.0288  -0.0004 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2179 0.1252 0.2494 -0.0509 0.0238  -0.0073 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2546 0.1698 0.2468 -0.0748 0.0095  0.0093  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2411 0.1609 0.2383 -0.0649 0.0084  0.0038  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2040 0.1127 0.2481 -0.0411 0.0223  -0.0115 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2419 0.1751 0.2225 -0.0684 -0.0050 0.0109  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2113 0.1310 0.2272 -0.0444 0.0109  -0.0086 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2246 0.1564 0.2119 -0.0572 -0.0011 0.0024  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1778 0.1106 0.3035 -0.0059 -0.0185 -0.0003 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1668 0.1051 0.2736 0.0016  -0.0356 0.0005  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1693 0.1236 0.2556 -0.0028 -0.0346 0.0073  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1672 0.1299 0.2580 -0.0098 -0.0321 0.0137  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1800 0.1056 0.2998 0.0114  -0.0553 0.0010  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1884 0.1165 0.3283 0.0149  -0.0590 0.0040  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2269 0.1641 0.3515 0.0179  -0.0560 0.0065  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2681 0.2155 0.4108 0.0183  -0.0538 0.0110  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2217 0.1549 0.3229 0.0201  -0.0532 0.0062  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1624 0.1202 0.2329 -0.0001 -0.0369 0.0096  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1581 0.1335 0.2310 -0.0037 -0.0366 0.0239  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1637 0.1317 0.2360 0.0089  -0.0322 0.0247  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1736 0.1358 0.2291 0.0089  -0.0293 0.0215  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1750 0.1596 0.2308 -0.0245 -0.0369 0.0330  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2429 0.2484 0.3144 -0.0343 -0.0460 0.0577  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2317 0.2464 0.3361 -0.0195 -0.0434 0.0669  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3020 0.3092 0.3533 -0.0595 -0.0548 0.0703  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1641 0.1251 0.2519 0.0188  -0.0264 0.0278  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1811 0.1186 0.2621 0.0289  -0.0097 0.0266  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1801 0.1174 0.2600 0.0287  -0.0101 0.0262  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1713 0.1270 0.2749 0.0280  0.0010  0.0436  36  SER   A C   
244  O O   . SER   A 30  ? 0.1861 0.1200 0.2733 0.0335  0.0164  0.0392  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1968 0.1195 0.2951 0.0368  0.0030  0.0288  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1949 0.1124 0.2858 0.0367  0.0023  0.0258  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2347 0.1465 0.3219 0.0356  -0.0113 0.0182  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.1887 0.1400 0.3285 0.0356  0.0004  0.0441  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1507 0.1428 0.2913 0.0179  -0.0092 0.0660  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1420 0.1544 0.3168 0.0130  -0.0068 0.0906  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1430 0.1528 0.2829 0.0061  -0.0123 0.0827  37  SER   A C   
252  O O   . SER   A 31  ? 0.1467 0.1642 0.3114 0.0067  -0.0054 0.0986  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1611 0.2076 0.3787 -0.0043 -0.0269 0.1224  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2297 0.2800 0.4033 -0.0272 -0.0494 0.1183  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1244 0.1231 0.2172 0.0004  -0.0216 0.0607  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1157 0.1090 0.1781 -0.0052 -0.0235 0.0517  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1499 0.1146 0.1835 0.0075  -0.0154 0.0304  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1668 0.1269 0.1805 0.0046  -0.0162 0.0240  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1364 0.1313 0.1722 -0.0246 -0.0340 0.0460  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1470 0.1573 0.1891 -0.0477 -0.0475 0.0685  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1903 0.1826 0.1859 -0.0729 -0.0490 0.0598  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1900 0.1679 0.1542 -0.0800 -0.0418 0.0483  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2371 0.1905 0.1533 -0.1084 -0.0379 0.0444  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2398 0.1779 0.1249 -0.1369 -0.0447 0.0541  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2717 0.2102 0.1646 -0.1124 -0.0269 0.0326  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1606 0.1020 0.1868 0.0173  -0.0117 0.0203  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1865 0.0907 0.1751 0.0209  -0.0137 0.0042  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1901 0.0992 0.1749 0.0139  -0.0303 -0.0027 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1865 0.0774 0.1504 0.0123  -0.0361 -0.0081 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2066 0.0869 0.1706 0.0245  0.0021  0.0028  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2874 0.1187 0.1970 0.0204  -0.0049 -0.0109 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2907 0.0920 0.1788 0.0168  -0.0138 -0.0168 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3304 0.1516 0.2173 0.0176  -0.0054 -0.0133 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1775 0.1072 0.1852 0.0082  -0.0342 -0.0006 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1605 0.0878 0.1775 0.0027  -0.0382 -0.0059 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1750 0.0962 0.2172 0.0042  -0.0452 -0.0065 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1950 0.1227 0.2445 0.0059  -0.0444 -0.0040 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1510 0.0916 0.1673 -0.0098 -0.0260 -0.0048 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1660 0.1112 0.1624 -0.0154 -0.0219 -0.0031 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1660 0.1098 0.1462 -0.0356 -0.0108 -0.0029 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1752 0.1078 0.1703 -0.0092 -0.0245 -0.0092 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1690 0.0797 0.2346 0.0031  -0.0521 -0.0062 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1769 0.0836 0.2836 0.0038  -0.0577 -0.0018 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1716 0.0763 0.3219 0.0005  -0.0461 0.0019  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1753 0.0754 0.3259 -0.0011 -0.0507 0.0040  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1848 0.0706 0.2892 0.0047  -0.0871 0.0037  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1913 0.0747 0.3506 0.0042  -0.0987 0.0137  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2205 0.0849 0.3585 0.0025  -0.1211 0.0154  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1791 0.0557 0.3960 -0.0008 -0.1139 0.0297  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1709 0.0753 0.3592 -0.0011 -0.0244 0.0027  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1737 0.0681 0.4174 -0.0034 -0.0001 0.0073  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1799 0.0710 0.4997 0.0015  -0.0083 0.0225  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1688 0.0623 0.4865 0.0034  -0.0089 0.0211  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2075 0.0882 0.4252 -0.0144 0.0456  -0.0051 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2093 0.0679 0.4902 -0.0162 0.0839  -0.0014 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2353 0.1195 0.3812 -0.0234 0.0455  -0.0147 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1971 0.0842 0.5904 0.0026  -0.0177 0.0409  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2075 0.0926 0.6958 0.0052  -0.0283 0.0641  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2347 0.1107 0.8191 0.0066  0.0124  0.0771  43  SER   A C   
300  O O   . SER   A 37  ? 0.2217 0.0925 0.7989 0.0044  0.0333  0.0718  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2046 0.0888 0.7049 -0.0003 -0.0906 0.0856  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2213 0.1022 0.7207 -0.0065 -0.1099 0.0950  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2493 0.1208 0.9310 0.0107  0.0266  0.0959  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2769 0.1341 1.0707 0.0137  0.0757  0.1121  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2909 0.1593 1.1923 0.0124  0.0373  0.1513  44  SER   A C   
306  O O   . SER   A 38  ? 0.2787 0.1599 1.1929 0.0065  -0.0307 0.1743  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2762 0.1217 1.1429 0.0190  0.1109  0.1204  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2991 0.1638 1.1960 0.0202  0.0515  0.1411  44  SER   A OG  
309  N N   . THR   A 39  ? 0.3178 0.1755 1.2988 0.0143  0.0811  0.1618  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3273 0.1969 1.4283 0.0115  0.0466  0.2055  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3513 0.2091 1.6257 0.0191  0.1027  0.2364  45  THR   A C   
312  O O   . THR   A 39  ? 0.3780 0.2072 1.6526 0.0255  0.1841  0.2136  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3492 0.2201 1.3976 0.0070  0.0427  0.1953  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3672 0.2145 1.4280 0.0119  0.1264  0.1754  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3983 0.2756 1.2826 0.0012  0.0025  0.1639  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3367 0.2102 1.7592 0.0155  0.0619  0.2907  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3145 0.1796 1.9334 0.0238  0.1149  0.3301  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3397 0.1910 2.0077 0.0268  0.1709  0.3300  46  THR   A C   
319  O O   . THR   A 40  ? 0.3423 0.1653 2.1153 0.0363  0.2605  0.3344  46  THR   A O   
320  C CB  . THR   A 40  ? 0.2725 0.1630 2.0422 0.0151  0.0359  0.3975  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.2924 0.1996 2.0252 -0.0028 -0.0498 0.4184  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.2863 0.1827 2.0153 0.0119  -0.0076 0.3966  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3560 0.2215 1.9478 0.0180  0.1238  0.3246  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3469 0.2021 1.9752 0.0198  0.1685  0.3239  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4095 0.2329 1.8744 0.0216  0.2377  0.2585  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4650 0.2848 1.7770 0.0188  0.2270  0.2185  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3426 0.2263 1.9677 0.0068  0.0799  0.3532  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4026 0.2006 1.9021 0.0234  0.3059  0.2510  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4594 0.2187 1.8088 0.0182  0.3691  0.1948  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4758 0.2580 1.6959 0.0111  0.3136  0.1750  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4502 0.2580 1.7334 0.0110  0.2723  0.2038  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4723 0.1826 1.9116 0.0199  0.4730  0.1946  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5923 0.2357 1.8825 0.0079  0.5590  0.1376  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6724 0.2833 1.9579 0.0075  0.6015  0.1279  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6521 0.2572 2.0998 0.0187  0.6345  0.1620  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7504 0.3412 1.8596 -0.0059 0.5985  0.0860  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.5120 0.2796 1.5591 0.0036  0.3210  0.1279  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.5251 0.3083 1.4414 -0.0030 0.2812  0.1048  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.5200 0.2623 1.3790 -0.0119 0.3496  0.0756  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.5441 0.2348 1.3576 -0.0213 0.4211  0.0498  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4959 0.2539 1.3456 -0.0127 0.3278  0.0790  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.5145 0.2327 1.3151 -0.0227 0.3891  0.0540  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.5279 0.2536 1.1713 -0.0335 0.3578  0.0242  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.5547 0.2517 1.1553 -0.0439 0.3958  0.0071  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4998 0.2208 1.4408 -0.0155 0.4099  0.0839  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.5413 0.2495 1.6975 -0.0036 0.4584  0.1268  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.5020 0.2623 1.0647 -0.0321 0.2931  0.0195  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.5149 0.2834 0.9465 -0.0413 0.2662  -0.0032 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.5382 0.2576 0.8670 -0.0627 0.3158  -0.0336 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.5599 0.2541 0.8793 -0.0685 0.3418  -0.0398 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.5370 0.3472 0.9194 -0.0343 0.1949  0.0014  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.5490 0.3943 0.9692 -0.0242 0.1363  0.0243  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.5548 0.4029 0.9905 -0.0246 0.1369  0.0292  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.5488 0.4125 0.9737 -0.0191 0.0901  0.0370  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.5471 0.2496 0.7942 -0.0779 0.3249  -0.0502 52  THR   A N   
356  C CA  . THR   A 46  ? 0.5871 0.2347 0.7185 -0.1080 0.3619  -0.0755 52  THR   A CA  
357  C C   . THR   A 46  ? 0.5742 0.2537 0.6129 -0.1148 0.3031  -0.0780 52  THR   A C   
358  O O   . THR   A 46  ? 0.5674 0.2914 0.6039 -0.1037 0.2568  -0.0700 52  THR   A O   
359  C CB  . THR   A 46  ? 0.6350 0.2393 0.7407 -0.1244 0.4066  -0.0879 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.6629 0.2128 0.8392 -0.1260 0.4842  -0.0901 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.6872 0.2480 0.6455 -0.1613 0.4104  -0.1087 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.5691 0.2253 0.5401 -0.1327 0.3063  -0.0859 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.5601 0.2449 0.4580 -0.1413 0.2540  -0.0826 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.5950 0.2376 0.3871 -0.1786 0.2623  -0.0926 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.6355 0.2050 0.3699 -0.2094 0.3135  -0.1076 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.5614 0.2475 0.4458 -0.1436 0.2440  -0.0801 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.5144 0.2307 0.5024 -0.1119 0.2402  -0.0698 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.5687 0.2895 0.3985 -0.1503 0.1896  -0.0706 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.4713 0.2476 0.5151 -0.0836 0.1887  -0.0548 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.5630 0.2434 0.3278 -0.1792 0.2150  -0.0830 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.6002 0.2463 0.2705 -0.2174 0.2097  -0.0850 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.6358 0.2531 0.2240 -0.2529 0.1936  -0.0798 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.6026 0.2596 0.2168 -0.2393 0.1621  -0.0673 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.5668 0.2661 0.2520 -0.2048 0.1640  -0.0709 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.7112 0.2545 0.1955 -0.3022 0.2138  -0.0879 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.7769 0.2806 0.1660 -0.3479 0.1924  -0.0786 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.8235 0.3115 0.1397 -0.3871 0.1563  -0.0649 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.8939 0.3057 0.1270 -0.4249 0.1893  -0.0801 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.8545 0.2596 0.1674 -0.3816 0.2559  -0.1012 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.8359 0.2537 0.2341 -0.3433 0.2959  -0.1116 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.8049 0.2964 0.2671 -0.3138 0.2491  -0.0935 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.7646 0.2649 0.3133 -0.2788 0.2871  -0.1021 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.7061 0.2726 0.3371 -0.2420 0.2565  -0.0901 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.6498 0.2765 0.2875 -0.2336 0.1951  -0.0715 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.6747 0.2439 0.3860 -0.2150 0.2891  -0.0946 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.7700 0.3296 0.1276 -0.3761 0.0920  -0.0348 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.7824 0.3428 0.1028 -0.4057 0.0522  -0.0145 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.7456 0.3836 0.1306 -0.3931 -0.0135 0.0253  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.6873 0.3739 0.1388 -0.3607 -0.0232 0.0327  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.7560 0.3331 0.1198 -0.3773 0.0764  -0.0296 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.6453 0.3269 0.1550 -0.3009 0.0644  -0.0246 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.7621 0.4128 0.1406 -0.4150 -0.0540 0.0517  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.7205 0.4428 0.1801 -0.4014 -0.1080 0.0937  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.6656 0.4343 0.1923 -0.3702 -0.1116 0.0991  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.6527 0.4552 0.2216 -0.3787 -0.1535 0.1371  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.7983 0.4958 0.2051 -0.4640 -0.1654 0.1368  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.9597 0.6106 0.2912 -0.5206 -0.1944 0.1546  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 1.0072 0.6335 0.3099 -0.5155 -0.1622 0.1271  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 1.0412 0.6784 0.3439 -0.5733 -0.2530 0.1993  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.6331 0.4008 0.1740 -0.3359 -0.0671 0.0641  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.5707 0.3772 0.1700 -0.3025 -0.0626 0.0630  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.4899 0.3646 0.1856 -0.2642 -0.0843 0.0877  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.4856 0.3806 0.2156 -0.2415 -0.0807 0.0865  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.5669 0.3645 0.1787 -0.2694 -0.0138 0.0253  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.6365 0.3598 0.1661 -0.3037 0.0249  -0.0019 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.4276 0.3318 0.1664 -0.2572 -0.1015 0.1091  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.3509 0.3090 0.1829 -0.2197 -0.1087 0.1311  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2977 0.2713 0.1603 -0.1840 -0.0841 0.1150  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2612 0.2665 0.1893 -0.1603 -0.0855 0.1346  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3564 0.3376 0.2351 -0.2441 -0.1515 0.1832  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.4227 0.4100 0.3162 -0.2632 -0.1784 0.2105  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.4452 0.4635 0.4161 -0.2829 -0.2220 0.2710  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4960 0.4946 0.4329 -0.3363 -0.2674 0.3035  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3813 0.4430 0.4598 -0.2434 -0.2088 0.2911  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.3028 0.2498 0.1209 -0.1827 -0.0597 0.0827  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2705 0.2299 0.1151 -0.1508 -0.0392 0.0684  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2572 0.1961 0.0817 -0.1369 -0.0110 0.0348  60  THR   A C   
418  O O   . THR   A 54  ? 0.2908 0.1975 0.0734 -0.1581 -0.0001 0.0205  60  THR   A O   
419  C CB  . THR   A 54  ? 0.3251 0.2780 0.1566 -0.1672 -0.0441 0.0744  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.4085 0.3175 0.1736 -0.1962 -0.0315 0.0533  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.3125 0.2826 0.1699 -0.1894 -0.0782 0.1148  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2183 0.1710 0.0746 -0.1039 0.0012  0.0255  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2137 0.1525 0.0712 -0.0906 0.0201  0.0033  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1994 0.1500 0.0846 -0.0620 0.0218  0.0017  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2033 0.1661 0.0976 -0.0538 0.0173  0.0126  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1860 0.1282 0.0840 -0.0498 0.0273  -0.0089 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1836 0.1251 0.0939 -0.0312 0.0222  -0.0079 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1758 0.1101 0.0911 -0.0228 0.0138  -0.0092 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1588 0.0891 0.0878 -0.0280 0.0174  -0.0142 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1964 0.1306 0.1247 -0.0329 0.0298  -0.0127 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2076 0.1359 0.1431 -0.0212 0.0168  -0.0070 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1943 0.1307 0.1121 -0.0444 0.0402  -0.0136 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1859 0.1112 0.0866 -0.0122 0.0061  -0.0052 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1798 0.0894 0.0756 -0.0086 -0.0047 -0.0061 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2122 0.0956 0.0920 -0.0088 -0.0198 -0.0027 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2240 0.0982 0.0858 -0.0084 -0.0181 -0.0003 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1808 0.0882 0.0620 -0.0034 0.0001  -0.0043 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2144 0.1001 0.0676 0.0037  0.0105  -0.0009 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2249 0.1224 0.0871 0.0069  0.0246  0.0062  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2607 0.1063 0.0757 0.0045  0.0095  -0.0040 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2649 0.1368 0.1089 0.0146  0.0446  0.0102  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3089 0.1189 0.0879 0.0083  0.0307  -0.0034 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3200 0.1438 0.1179 0.0151  0.0514  0.0035  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3853 0.1686 0.1548 0.0199  0.0819  0.0049  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2158 0.0844 0.1010 -0.0127 -0.0378 0.0003  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2630 0.0990 0.1260 -0.0215 -0.0627 0.0095  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3072 0.1005 0.1016 -0.0249 -0.0643 0.0061  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.2906 0.0816 0.0798 -0.0216 -0.0591 0.0010  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2661 0.1043 0.1809 -0.0293 -0.0872 0.0222  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.3213 0.1213 0.2097 -0.0461 -0.1245 0.0393  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.3527 0.1424 0.2297 -0.0530 -0.1335 0.0480  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.3674 0.1349 0.2303 -0.0593 -0.1532 0.0477  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.4073 0.1545 0.2500 -0.0756 -0.1739 0.0676  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.4299 0.1508 0.2518 -0.0838 -0.1943 0.0666  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.4634 0.1725 0.2716 -0.0932 -0.2054 0.0770  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.5595 0.2147 0.3152 -0.1241 -0.2508 0.0985  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.3591 0.1131 0.0964 -0.0324 -0.0650 0.0077  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.4387 0.1328 0.0953 -0.0396 -0.0549 0.0019  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.5180 0.1503 0.1111 -0.0671 -0.0917 0.0121  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.5368 0.1431 0.0957 -0.0790 -0.1006 0.0186  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.4671 0.1506 0.0985 -0.0293 -0.0155 -0.0046 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.5688 0.1570 0.0924 -0.0411 0.0138  -0.0129 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.5581 0.1683 0.1398 -0.0805 -0.1186 0.0171  66  SER   A N   
464  C CA  . SER   A 60  ? 0.6380 0.1880 0.1626 -0.1142 -0.1655 0.0337  66  SER   A CA  
465  C C   . SER   A 60  ? 0.7321 0.1899 0.1273 -0.1378 -0.1557 0.0273  66  SER   A C   
466  O O   . SER   A 60  ? 0.7842 0.1958 0.1292 -0.1683 -0.1943 0.0443  66  SER   A O   
467  C CB  . SER   A 60  ? 0.6918 0.2333 0.2296 -0.1258 -0.1971 0.0422  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.7827 0.3042 0.2816 -0.1170 -0.1651 0.0227  66  SER   A OG  
469  N N   . SER   A 61  ? 0.7659 0.1922 0.1092 -0.1261 -0.1020 0.0055  67  SER   A N   
470  C CA  . SER   A 61  ? 0.8640 0.1887 0.0787 -0.1476 -0.0740 -0.0046 67  SER   A CA  
471  C C   . SER   A 61  ? 0.8810 0.1974 0.0758 -0.1487 -0.0623 -0.0017 67  SER   A C   
472  O O   . SER   A 61  ? 0.9736 0.1970 0.0540 -0.1715 -0.0409 -0.0081 67  SER   A O   
473  C CB  . SER   A 61  ? 0.8955 0.1903 0.0840 -0.1314 -0.0099 -0.0254 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.8551 0.2167 0.1283 -0.0947 0.0353  -0.0302 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.7961 0.2016 0.0954 -0.1270 -0.0743 0.0074  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.7853 0.1994 0.0874 -0.1256 -0.0701 0.0128  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.7573 0.2218 0.1302 -0.1329 -0.1248 0.0355  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.7587 0.2326 0.1398 -0.1336 -0.1271 0.0427  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.7195 0.1971 0.0947 -0.0885 -0.0201 0.0022  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.7830 0.2155 0.1144 -0.0781 0.0419  -0.0127 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.9000 0.2378 0.1217 -0.0981 0.0686  -0.0170 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.9525 0.2452 0.1505 -0.0850 0.1404  -0.0294 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 1.0484 0.2536 0.1624 -0.0998 0.1714  -0.0411 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 1.0899 0.2416 0.1242 -0.1314 0.1300  -0.0423 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 1.0650 0.2302 0.1764 -0.0851 0.2460  -0.0495 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.7202 0.2193 0.1565 -0.1363 -0.1637 0.0485  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.6712 0.2232 0.2047 -0.1388 -0.2055 0.0730  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.5888 0.2103 0.2036 -0.1102 -0.1751 0.0668  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.5743 0.2093 0.2240 -0.1166 -0.1942 0.0835  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.7479 0.2436 0.2333 -0.1798 -0.2634 0.1026  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.8819 0.3149 0.3044 -0.2140 -0.3067 0.1157  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 1.0104 0.3976 0.4073 -0.2594 -0.3769 0.1552  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 1.1901 0.4820 0.4684 -0.3054 -0.4174 0.1652  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.3503 0.5409 0.4892 -0.3539 -0.4473 0.1765  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.3735 0.5503 0.4806 -0.3591 -0.4398 0.1793  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.4541 0.5489 0.4746 -0.4008 -0.4839 0.1845  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.5315 0.1908 0.1699 -0.0821 -0.1288 0.0447  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.4694 0.1828 0.1650 -0.0605 -0.0995 0.0378  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.3939 0.1593 0.1479 -0.0400 -0.0742 0.0255  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.4008 0.1578 0.1374 -0.0369 -0.0666 0.0180  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.5270 0.2126 0.1612 -0.0555 -0.0664 0.0276  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.6287 0.2857 0.2289 -0.0696 -0.0800 0.0383  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.7575 0.3648 0.2794 -0.0687 -0.0428 0.0280  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.8389 0.4186 0.3259 -0.0829 -0.0544 0.0384  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.9521 0.4365 0.3162 -0.1033 -0.0371 0.0337  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.3221 0.1342 0.1368 -0.0297 -0.0607 0.0240  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2749 0.1256 0.1277 -0.0181 -0.0379 0.0137  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2807 0.1400 0.1152 -0.0097 -0.0126 0.0082  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2916 0.1458 0.1158 -0.0097 -0.0086 0.0114  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2462 0.1272 0.1662 -0.0190 -0.0349 0.0155  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2279 0.1047 0.1930 -0.0255 -0.0554 0.0271  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2456 0.1313 0.2402 -0.0240 -0.0498 0.0235  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2300 0.0934 0.2198 -0.0352 -0.0836 0.0466  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2225 0.1024 0.2672 -0.0305 -0.0713 0.0408  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2269 0.0941 0.2728 -0.0387 -0.0955 0.0574  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2530 0.1260 0.0908 -0.0036 0.0027  0.0041  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2509 0.1362 0.0913 0.0027  0.0230  0.0072  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2199 0.1409 0.0951 -0.0009 0.0257  0.0091  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1937 0.1218 0.0771 -0.0043 0.0212  0.0067  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2786 0.1367 0.0925 0.0097  0.0405  0.0092  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.3383 0.1420 0.0934 0.0068  0.0460  0.0067  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.3641 0.1521 0.1025 0.0085  0.0607  0.0099  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.3905 0.1499 0.0975 -0.0009 0.0385  0.0017  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.4268 0.1513 0.0939 0.0000  0.0678  0.0071  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.4576 0.1511 0.0894 -0.0124 0.0417  -0.0003 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.4784 0.1517 0.0864 -0.0126 0.0581  0.0018  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.5937 0.1881 0.1106 -0.0291 0.0648  -0.0009 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2185 0.1571 0.1084 -0.0042 0.0311  0.0147  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2083 0.1693 0.1156 -0.0167 0.0283  0.0205  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2247 0.1950 0.1502 -0.0130 0.0307  0.0370  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2377 0.2008 0.1726 -0.0001 0.0447  0.0459  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2190 0.1884 0.1318 -0.0237 0.0301  0.0248  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2388 0.1975 0.1480 -0.0081 0.0392  0.0275  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2258 0.1592 0.1112 0.0001  0.0379  0.0184  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2053 0.1868 0.1390 -0.0249 0.0207  0.0428  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2054 0.1997 0.1720 -0.0237 0.0194  0.0643  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2002 0.2109 0.1768 -0.0498 -0.0022 0.0818  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2226 0.2237 0.1632 -0.0693 -0.0110 0.0691  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2298 0.2138 0.1934 -0.0130 0.0249  0.0579  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2604 0.2174 0.2139 0.0073  0.0477  0.0518  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2473 0.2239 0.1815 -0.0212 0.0151  0.0385  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1790 0.2081 0.2056 -0.0531 -0.0095 0.1138  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1876 0.2299 0.2296 -0.0818 -0.0384 0.1403  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1804 0.2278 0.2502 -0.0694 -0.0329 0.1462  75  SER   A C   
545  O O   . SER   A 69  ? 0.2000 0.2461 0.3048 -0.0419 -0.0069 0.1475  75  SER   A O   
546  C CB  . SER   A 69  ? 0.1871 0.2507 0.2916 -0.0915 -0.0531 0.1818  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2586 0.3165 0.3375 -0.1021 -0.0573 0.1760  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1625 0.2070 0.2078 -0.0895 -0.0514 0.1457  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1590 0.2092 0.2312 -0.0788 -0.0475 0.1513  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1882 0.2524 0.2843 -0.1094 -0.0811 0.1863  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2219 0.2804 0.2883 -0.1456 -0.1102 0.2001  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1675 0.1972 0.1889 -0.0663 -0.0326 0.1131  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1772 0.1883 0.1364 -0.0895 -0.0410 0.0921  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1878 0.1842 0.1154 -0.0877 -0.0295 0.0702  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2028 0.2053 0.1366 -0.1138 -0.0552 0.0948  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2316 0.2031 0.1109 -0.1071 -0.0251 0.0505  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2466 0.2191 0.1198 -0.1361 -0.0508 0.0739  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2552 0.2114 0.1047 -0.1326 -0.0331 0.0521  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1740 0.2523 0.3242 -0.0990 -0.0790 0.2052  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1751 0.2689 0.3595 -0.1294 -0.1155 0.2459  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2071 0.2803 0.3157 -0.1547 -0.1322 0.2275  77  SER   A C   
562  O O   . SER   A 71  ? 0.2243 0.2764 0.2742 -0.1416 -0.1098 0.1850  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1683 0.2867 0.4591 -0.1077 -0.1026 0.2794  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2063 0.3121 0.4809 -0.0796 -0.0711 0.2483  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2243 0.2999 0.3355 -0.1936 -0.1720 0.2624  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2859 0.3344 0.3221 -0.2210 -0.1845 0.2480  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2833 0.3452 0.3556 -0.1907 -0.1648 0.2382  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2497 0.3413 0.4127 -0.1636 -0.1547 0.2600  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3410 0.3793 0.3586 -0.2797 -0.2387 0.2932  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4319 0.4402 0.3832 -0.3165 -0.2565 0.2940  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5772 0.5452 0.4534 -0.3903 -0.3107 0.3269  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.7100 0.6325 0.4953 -0.4215 -0.3111 0.3092  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.8111 0.6814 0.5089 -0.5002 -0.3653 0.3424  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.3215 0.3584 0.3291 -0.1929 -0.1529 0.2052  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.3153 0.3646 0.3585 -0.1636 -0.1353 0.1959  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.3017 0.3783 0.4186 -0.1735 -0.1605 0.2426  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.3068 0.3816 0.4156 -0.2165 -0.2012 0.2784  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3610 0.3765 0.3245 -0.1731 -0.1239 0.1598  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.4026 0.3823 0.2871 -0.2160 -0.1368 0.1573  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3663 0.3578 0.2708 -0.2212 -0.1488 0.1752  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2783 0.3764 0.4713 -0.1366 -0.1367 0.2471  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2559 0.3824 0.5426 -0.1400 -0.1523 0.2946  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2402 0.3708 0.5771 -0.0986 -0.1123 0.2807  80  SER   A C   
584  O O   . SER   A 74  ? 0.2460 0.3544 0.5340 -0.0727 -0.0803 0.2356  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2581 0.4096 0.6302 -0.1510 -0.1710 0.3457  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.2971 0.4490 0.7041 -0.1154 -0.1305 0.3321  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2169 0.3712 0.6475 -0.0975 -0.1176 0.3215  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2190 0.3713 0.7024 -0.0632 -0.0774 0.3139  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2059 0.3549 0.7588 -0.0356 -0.0354 0.3230  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1924 0.3673 0.8448 -0.0437 -0.0453 0.3738  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1900 0.3702 0.7633 -0.0765 -0.0992 0.3630  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2348 0.4120 0.7517 -0.0967 -0.1270 0.3538  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2150 0.4235 0.8255 -0.1207 -0.1627 0.4158  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2598 0.4148 0.7389 -0.0651 -0.0880 0.3068  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2208 0.3344 0.7292 -0.0058 0.0117  0.2794  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2160 0.3095 0.7715 0.0189  0.0620  0.2822  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2483 0.3018 0.8054 0.0449  0.1159  0.2602  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2625 0.2913 0.7343 0.0473  0.1144  0.2209  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2466 0.3193 0.7200 0.0205  0.0655  0.2498  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2354 0.3422 0.7356 -0.0035 0.0251  0.2821  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2660 0.2936 0.7369 0.0468  0.1261  0.2317  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.2867 0.3808 0.6967 -0.0104 0.0134  0.2504  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2535 0.2956 0.9112 0.0622  0.1657  0.2878  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3144 0.3028 0.9613 0.0830  0.2252  0.2644  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.3765 0.2936 0.8949 0.0920  0.2604  0.2091  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.3912 0.2919 0.8888 0.0943  0.2751  0.2038  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3035 0.2878 1.0945 0.0984  0.2807  0.3083  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.3663 0.2829 1.1473 0.1171  0.3529  0.2855  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.3792 0.3004 1.1726 0.1170  0.3474  0.2848  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.4288 0.2700 1.1842 0.1319  0.4296  0.2655  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.4229 0.2742 1.2015 0.1312  0.4162  0.2633  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.4749 0.2383 1.2087 0.1433  0.5019  0.2439  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.4635 0.2324 1.2071 0.1427  0.4937  0.2420  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.4198 0.2938 0.8520 0.0933  0.2685  0.1714  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.4968 0.2971 0.8018 0.0935  0.2909  0.1246  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.5517 0.2744 0.8330 0.1011  0.3525  0.1084  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.5262 0.2535 0.8260 0.1018  0.3491  0.1093  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.5273 0.3402 0.7352 0.0798  0.2321  0.0949  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.5986 0.3374 0.6840 0.0745  0.2444  0.0560  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.5004 0.3784 0.7280 0.0700  0.1813  0.1093  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.6191 0.2631 0.8514 0.1043  0.4115  0.0924  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.6927 0.2350 0.8753 0.1057  0.4839  0.0720  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.7491 0.2468 0.8120 0.0902  0.4567  0.0363  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.7661 0.2850 0.7549 0.0775  0.3940  0.0195  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.8012 0.2593 0.9098 0.1025  0.5377  0.0545  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.8755 0.3307 1.1058 0.1205  0.6075  0.0873  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 1.0274 0.3854 1.2709 0.1271  0.7075  0.0834  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 1.0769 0.3849 1.2543 0.1186  0.7162  0.0604  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 1.0554 0.3838 1.3795 0.1404  0.7810  0.1043  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.7726 0.2049 0.8210 0.0902  0.5054  0.0266  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.8291 0.2120 0.7656 0.0726  0.4800  -0.0043 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.9118 0.2168 0.6833 0.0467  0.4581  -0.0384 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.9575 0.2093 0.6784 0.0414  0.4908  -0.0456 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.8530 0.1605 0.7924 0.0743  0.5485  -0.0102 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.9234 0.2237 0.6192 0.0291  0.4000  -0.0548 87  SER   A N   
636  C CA  . SER   A 81  ? 0.9790 0.2124 0.5312 -0.0006 0.3632  -0.0783 87  SER   A CA  
637  C C   . SER   A 81  ? 1.0149 0.2040 0.4938 -0.0218 0.3312  -0.0929 87  SER   A C   
638  O O   . SER   A 81  ? 0.9736 0.1954 0.5194 -0.0092 0.3375  -0.0864 87  SER   A O   
639  C CB  . SER   A 81  ? 0.9459 0.2654 0.5246 0.0015  0.2949  -0.0688 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.9059 0.3194 0.5600 0.0109  0.2405  -0.0569 87  SER   A OG  
641  N N   . GLU   A 82  ? 1.0791 0.1963 0.4265 -0.0561 0.2913  -0.1085 88  GLU   A N   
642  C CA  . GLU   A 82  ? 1.1162 0.1977 0.4037 -0.0792 0.2494  -0.1161 88  GLU   A CA  
643  C C   . GLU   A 82  ? 1.0016 0.2028 0.3911 -0.0635 0.1813  -0.0995 88  GLU   A C   
644  O O   . GLU   A 82  ? 1.0156 0.2038 0.3796 -0.0787 0.1420  -0.1010 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.2837 0.2546 0.4087 -0.1269 0.2144  -0.1287 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.4662 0.3203 0.4737 -0.1482 0.2701  -0.1440 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.5736 0.4629 0.5795 -0.1494 0.2379  -0.1353 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.4775 0.4956 0.6104 -0.1183 0.2058  -0.1182 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.7281 0.5095 0.5984 -0.1845 0.2458  -0.1456 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.8912 0.2008 0.3894 -0.0365 0.1681  -0.0835 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.7921 0.2046 0.3794 -0.0234 0.1156  -0.0694 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.6991 0.1837 0.3995 0.0042  0.1416  -0.0561 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.6676 0.2017 0.4173 0.0094  0.1130  -0.0496 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.7493 0.2182 0.3617 -0.0203 0.0821  -0.0610 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.8028 0.2042 0.3148 -0.0477 0.0572  -0.0681 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.8433 0.2153 0.3082 -0.0731 0.0029  -0.0662 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.8407 0.2077 0.3105 -0.0506 0.0847  -0.0722 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.9109 0.2208 0.2880 -0.1036 -0.0288 -0.0653 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.9120 0.2140 0.2852 -0.0795 0.0585  -0.0760 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.9567 0.2310 0.2838 -0.1074 -0.0012 -0.0710 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 1.0450 0.2554 0.2813 -0.1408 -0.0352 -0.0678 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.6529 0.1447 0.4008 0.0200  0.1926  -0.0479 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.5751 0.1390 0.4415 0.0417  0.2086  -0.0260 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.6147 0.1396 0.5194 0.0528  0.2800  -0.0187 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.6590 0.1239 0.5222 0.0501  0.3229  -0.0259 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.4805 0.1317 0.4194 0.0513  0.1838  -0.0061 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.4231 0.1171 0.3436 0.0431  0.1252  -0.0102 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.4167 0.1098 0.3018 0.0372  0.1100  -0.0150 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.3905 0.1282 0.3409 0.0424  0.0904  -0.0066 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.3920 0.1218 0.2736 0.0308  0.0644  -0.0166 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.3692 0.1409 0.3143 0.0359  0.0480  -0.0087 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.3676 0.1355 0.2822 0.0305  0.0367  -0.0132 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.3098 0.1065 0.2292 0.0247  0.0024  -0.0140 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.5899 0.1552 0.5910 0.0665  0.2958  0.0009  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.5907 0.1332 0.6671 0.0806  0.3673  0.0183  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.5638 0.1718 0.7320 0.0918  0.3664  0.0486  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.5358 0.2064 0.7038 0.0874  0.3098  0.0538  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.5539 0.1378 0.7186 0.0897  0.3661  0.0369  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.5176 0.1851 0.6951 0.0853  0.2892  0.0432  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.5371 0.1744 0.5960 0.0698  0.2509  0.0133  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.5602 0.1547 0.8172 0.1052  0.4296  0.0723  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.5161 0.1755 0.8776 0.1139  0.4250  0.1090  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.4293 0.1970 0.8791 0.1114  0.3556  0.1424  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.4057 0.1936 0.8987 0.1127  0.3476  0.1526  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.5117 0.1400 0.9810 0.1295  0.5070  0.1364  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.3800 0.2065 0.8361 0.1036  0.3045  0.1549  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.3086 0.2176 0.8140 0.0924  0.2386  0.1810  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2777 0.2353 0.7991 0.0811  0.1987  0.2009  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.3032 0.2347 0.7875 0.0845  0.2170  0.1878  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.3221 0.2270 0.7309 0.0833  0.1987  0.1466  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3542 0.2554 0.6631 0.0731  0.1634  0.1172  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3875 0.2462 0.5965 0.0695  0.1528  0.0779  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.3776 0.2579 0.5338 0.0585  0.1082  0.0640  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.3979 0.2621 0.5051 0.0552  0.1046  0.0509  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.3620 0.2459 0.4352 0.0459  0.0688  0.0408  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.4037 0.2279 0.4982 0.0610  0.1415  0.0486  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2316 0.2514 0.7908 0.0635  0.1424  0.2291  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2191 0.2720 0.7649 0.0462  0.1012  0.2413  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2068 0.2515 0.6349 0.0352  0.0683  0.2003  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2109 0.2641 0.6128 0.0271  0.0451  0.1919  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2042 0.3138 0.8385 0.0238  0.0567  0.2962  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2107 0.3390 0.9894 0.0313  0.0811  0.3501  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2281 0.3692 1.0606 0.0284  0.0823  0.3784  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2165 0.3503 1.0895 0.0413  0.1043  0.3763  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2073 0.3687 1.1946 0.0348  0.1045  0.4360  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.1881 0.3409 1.2156 0.0484  0.1295  0.4325  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.1960 0.3625 1.2846 0.0455  0.1304  0.4634  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.1908 0.3779 1.4537 0.0530  0.1568  0.5257  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1899 0.2179 0.5556 0.0350  0.0687  0.1774  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1758 0.1988 0.4511 0.0242  0.0401  0.1456  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1429 0.2012 0.4227 -0.0012 0.0006  0.1671  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1374 0.2104 0.4558 -0.0065 -0.0020 0.1919  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2094 0.1918 0.4146 0.0343  0.0588  0.1112  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2088 0.1910 0.3453 0.0233  0.0309  0.0865  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2134 0.1523 0.2871 0.0316  0.0434  0.0565  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2273 0.1259 0.2797 0.0405  0.0650  0.0445  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1736 0.1141 0.2124 0.0249  0.0292  0.0455  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1163 0.1832 0.3598 -0.0199 -0.0284 0.1621  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1120 0.1940 0.3357 -0.0522 -0.0631 0.1797  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1483 0.2095 0.2946 -0.0579 -0.0628 0.1474  96  SER   A C   
721  O O   . SER   A 90  ? 0.1549 0.1958 0.2701 -0.0377 -0.0425 0.1149  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1226 0.2116 0.3376 -0.0755 -0.0887 0.1924  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.1637 0.2326 0.3294 -0.0654 -0.0766 0.1562  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1659 0.2285 0.2845 -0.0882 -0.0862 0.1604  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1971 0.2373 0.2477 -0.0986 -0.0832 0.1342  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1909 0.2276 0.2466 -0.0728 -0.0618 0.1172  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1863 0.2039 0.1995 -0.0669 -0.0500 0.0878  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2463 0.2620 0.2436 -0.1032 -0.0750 0.1048  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.3216 0.3314 0.3001 -0.1330 -0.0934 0.1205  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3941 0.3761 0.3084 -0.1749 -0.1071 0.1258  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.3302 0.3525 0.3398 -0.1298 -0.1001 0.1333  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.4068 0.3828 0.3096 -0.1976 -0.1230 0.1415  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.3754 0.3801 0.3410 -0.1700 -0.1207 0.1479  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1728 0.2256 0.2862 -0.0595 -0.0554 0.1394  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1788 0.2215 0.2954 -0.0365 -0.0311 0.1263  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1660 0.2202 0.2981 -0.0482 -0.0401 0.1462  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1389 0.2150 0.3200 -0.0654 -0.0600 0.1843  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1694 0.2081 0.3381 -0.0117 -0.0039 0.1345  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2076 0.2146 0.3576 0.0109  0.0300  0.1141  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2364 0.2158 0.3112 0.0137  0.0275  0.0767  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2198 0.2075 0.4109 0.0294  0.0651  0.1212  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1715 0.2110 0.2680 -0.0400 -0.0281 0.1242  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1783 0.2258 0.2824 -0.0501 -0.0350 0.1383  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1784 0.2144 0.2977 -0.0236 -0.0045 0.1307  99  MET   A C   
745  O O   . MET   A 93  ? 0.1980 0.2092 0.2723 -0.0097 0.0108  0.1000  99  MET   A O   
746  C CB  . MET   A 93  ? 0.2168 0.2495 0.2525 -0.0681 -0.0451 0.1151  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2634 0.2888 0.2624 -0.0977 -0.0650 0.1157  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.3109 0.3027 0.2306 -0.1189 -0.0594 0.0852  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2434 0.2245 0.1611 -0.0857 -0.0327 0.0502  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1557 0.2046 0.3369 -0.0195 0.0038  0.1603  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1739 0.2013 0.3626 0.0039  0.0408  0.1522  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1731 0.2045 0.3475 -0.0023 0.0344  0.1523  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1716 0.2273 0.3612 -0.0249 0.0039  0.1733  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1665 0.1977 0.4482 0.0180  0.0704  0.1859  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2120 0.2310 0.5151 0.0290  0.0898  0.1853  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2057 0.2196 0.6057 0.0448  0.1315  0.2169  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2613 0.2328 0.4779 0.0412  0.1118  0.1411  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1918 0.1941 0.3340 0.0145  0.0624  0.1311  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.2037 0.2048 0.3340 0.0137  0.0644  0.1292  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2201 0.1856 0.3554 0.0351  0.1099  0.1257  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2420 0.1713 0.3559 0.0465  0.1375  0.1125  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2384 0.2287 0.2936 0.0065  0.0482  0.0971  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2143 0.1818 0.3694 0.0378  0.1204  0.1364  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.2488 0.1718 0.3940 0.0548  0.1684  0.1302  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.3117 0.2015 0.3573 0.0520  0.1618  0.0942  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.3243 0.2380 0.3518 0.0422  0.1314  0.0885  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2399 0.1820 0.4603 0.0584  0.1819  0.1616  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.2700 0.1559 0.4726 0.0750  0.2400  0.1531  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1935 0.1748 0.5298 0.0561  0.1769  0.2074  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.3525 0.1847 0.3350 0.0568  0.1874  0.0729  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.4119 0.2079 0.3042 0.0492  0.1745  0.0463  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.4769 0.2036 0.2952 0.0462  0.1941  0.0278  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.5036 0.2176 0.3386 0.0506  0.2129  0.0304  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.5101 0.1866 0.2435 0.0352  0.1883  0.0114  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.5723 0.1701 0.2142 0.0226  0.1980  -0.0049 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.5691 0.1789 0.1978 0.0137  0.1579  -0.0120 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.5328 0.1945 0.1898 0.0108  0.1144  -0.0103 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.6423 0.1803 0.1937 0.0060  0.1934  -0.0141 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.7483 0.1879 0.1865 -0.0161 0.2020  -0.0283 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.8461 0.2104 0.2435 -0.0159 0.2629  -0.0350 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.8042 0.2123 0.1734 -0.0405 0.1554  -0.0337 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.9272 0.2065 0.2113 -0.0436 0.2521  -0.0482 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.9152 0.2216 0.1826 -0.0599 0.1826  -0.0453 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.6104 0.1653 0.1963 0.0087  0.1784  -0.0200 105 SER   A N   
785  C CA  . SER   A 99  ? 0.6303 0.1803 0.1924 -0.0020 0.1449  -0.0267 105 SER   A CA  
786  C C   . SER   A 99  ? 0.7191 0.1716 0.1922 -0.0159 0.1758  -0.0391 105 SER   A C   
787  O O   . SER   A 99  ? 0.7486 0.1553 0.2135 -0.0088 0.2350  -0.0409 105 SER   A O   
788  C CB  . SER   A 99  ? 0.5730 0.2003 0.2268 0.0126  0.1317  -0.0180 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.5897 0.2133 0.2849 0.0258  0.1747  -0.0113 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.7622 0.1768 0.1688 -0.0383 0.1375  -0.0459 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.8419 0.1568 0.1468 -0.0607 0.1527  -0.0582 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.8320 0.1775 0.1612 -0.0650 0.1085  -0.0564 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.7736 0.2035 0.1814 -0.0552 0.0660  -0.0463 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.9622 0.1792 0.1360 -0.0962 0.1399  -0.0636 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 1.0721 0.2463 0.2159 -0.0914 0.1962  -0.0678 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 1.2144 0.2942 0.2282 -0.1273 0.1852  -0.0713 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 1.2787 0.2722 0.1772 -0.1665 0.1554  -0.0752 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 1.2302 0.3197 0.2549 -0.1194 0.2030  -0.0679 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.8817 0.1635 0.1561 -0.0769 0.1244  -0.0658 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.8511 0.1736 0.1674 -0.0759 0.0861  -0.0623 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.8244 0.1869 0.1601 -0.0894 0.0130  -0.0500 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.7622 0.2055 0.1903 -0.0728 -0.0098 -0.0424 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.9270 0.1465 0.1458 -0.0976 0.1103  -0.0755 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.9869 0.1285 0.1470 -0.0979 0.1825  -0.0869 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.9544 0.1244 0.1349 -0.0894 0.1874  -0.0807 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.8551 0.1602 0.1109 -0.1203 -0.0212 -0.0450 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.8144 0.1550 0.1055 -0.1345 -0.0900 -0.0258 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.7161 0.1581 0.1214 -0.1088 -0.0996 -0.0159 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.6871 0.1659 0.1471 -0.1154 -0.1466 0.0016  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.6616 0.1441 0.1061 -0.0819 -0.0540 -0.0244 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.5778 0.1460 0.1164 -0.0609 -0.0571 -0.0178 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.4893 0.1297 0.1185 -0.0426 -0.0600 -0.0160 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.4295 0.1286 0.1263 -0.0326 -0.0663 -0.0108 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.5736 0.1547 0.1189 -0.0444 -0.0138 -0.0233 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.6238 0.1520 0.1001 -0.0602 -0.0142 -0.0225 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.6318 0.1456 0.0886 -0.0803 -0.0576 -0.0123 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.6561 0.1514 0.0985 -0.0547 0.0296  -0.0294 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.4865 0.1162 0.1114 -0.0400 -0.0513 -0.0212 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.4290 0.1166 0.1276 -0.0265 -0.0541 -0.0194 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.3793 0.0970 0.1285 -0.0324 -0.0912 -0.0086 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.4135 0.0961 0.1384 -0.0513 -0.1255 0.0011  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.4594 0.1185 0.1357 -0.0272 -0.0445 -0.0250 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.5040 0.1494 0.1726 -0.0119 0.0127  -0.0318 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.3221 0.0972 0.1399 -0.0200 -0.0832 -0.0074 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.2969 0.0960 0.1747 -0.0236 -0.1040 0.0028  111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2862 0.1041 0.1897 -0.0230 -0.1004 0.0067  111 GLY   A C   
827  O O   . GLY   A 105 ? 0.2589 0.1009 0.2247 -0.0221 -0.1004 0.0131  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.2950 0.1002 0.1551 -0.0227 -0.0902 0.0023  112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2629 0.0872 0.1456 -0.0214 -0.0842 0.0047  112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2061 0.0707 0.1279 -0.0127 -0.0582 -0.0022 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1981 0.0736 0.1096 -0.0077 -0.0434 -0.0082 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1744 0.0549 0.1401 -0.0146 -0.0530 0.0007  113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1620 0.0633 0.1492 -0.0147 -0.0271 -0.0069 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1594 0.0703 0.1190 -0.0155 -0.0131 -0.0116 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1699 0.0762 0.1193 -0.0142 -0.0178 -0.0087 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1816 0.0828 0.2318 -0.0183 -0.0188 -0.0015 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2073 0.1053 0.2976 -0.0179 -0.0219 0.0035  113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.1913 0.0953 0.2473 -0.0241 0.0142  -0.0106 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.1900 0.0845 0.3662 -0.0195 -0.0146 0.0177  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1482 0.0698 0.0967 -0.0209 0.0006  -0.0159 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1724 0.1029 0.1017 -0.0281 0.0095  -0.0155 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1872 0.1082 0.1199 -0.0439 0.0286  -0.0227 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1796 0.0908 0.1144 -0.0516 0.0383  -0.0270 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1741 0.1161 0.0891 -0.0310 0.0058  -0.0082 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1991 0.1505 0.1017 -0.0458 0.0068  0.0003  114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2046 0.1604 0.1090 -0.0381 0.0077  0.0044  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2139 0.1789 0.1215 -0.0515 -0.0030 0.0162  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.2095 0.1259 0.1386 -0.0503 0.0390  -0.0252 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2427 0.1360 0.1677 -0.0674 0.0661  -0.0345 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2644 0.1505 0.1473 -0.0866 0.0698  -0.0351 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2267 0.1296 0.1119 -0.0790 0.0574  -0.0286 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2741 0.1623 0.2460 -0.0583 0.0779  -0.0350 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3383 0.2218 0.3666 -0.0492 0.0823  -0.0311 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3806 0.2595 0.4681 -0.0448 0.0941  -0.0245 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4250 0.2959 0.5862 -0.0403 0.1053  -0.0155 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4354 0.2789 0.6228 -0.0483 0.1502  -0.0228 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.4325 0.2459 0.5629 -0.0660 0.1872  -0.0415 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.4265 0.2658 0.6954 -0.0418 0.1598  -0.0098 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.3180 0.1706 0.1611 -0.1140 0.0905  -0.0432 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.3826 0.2154 0.1760 -0.1408 0.0933  -0.0434 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.4365 0.2229 0.2223 -0.1542 0.1382  -0.0610 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.4193 0.2003 0.2572 -0.1378 0.1628  -0.0673 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.4227 0.2401 0.1571 -0.1725 0.0763  -0.0347 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.4664 0.2321 0.1586 -0.1966 0.1049  -0.0486 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.5061 0.2554 0.2335 -0.1853 0.1507  -0.0665 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.5716 0.2647 0.2863 -0.2008 0.2035  -0.0850 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.6199 0.2617 0.3184 -0.2144 0.2456  -0.0987 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.6412 0.2430 0.3685 -0.2139 0.2998  -0.1117 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.6588 0.3066 0.2887 -0.2414 0.2079  -0.0895 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.7764 0.3828 0.3076 -0.2868 0.1905  -0.0855 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.9129 0.4844 0.3628 -0.3296 0.1729  -0.0797 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.9272 0.5455 0.3894 -0.3282 0.1215  -0.0557 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.9922 0.4755 0.3589 -0.3705 0.2176  -0.0999 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.6303 0.2702 0.2888 -0.2270 0.2251  -0.0940 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.6403 0.2269 0.2730 -0.2430 0.2650  -0.1065 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.5691 0.1919 0.2990 -0.2045 0.2712  -0.1027 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.5915 0.1729 0.3172 -0.2130 0.3090  -0.1116 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.7031 0.2653 0.2419 -0.2803 0.2373  -0.1004 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.8019 0.3246 0.2402 -0.3273 0.2183  -0.0962 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.8176 0.3935 0.2601 -0.3273 0.1567  -0.0715 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.9012 0.3292 0.2285 -0.3803 0.2518  -0.1106 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.8861 0.4074 0.2324 -0.3784 0.1476  -0.0682 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.9353 0.3628 0.2002 -0.4138 0.2030  -0.0930 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.4734 0.1661 0.2818 -0.1668 0.2331  -0.0882 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.4034 0.1258 0.2962 -0.1366 0.2296  -0.0808 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.3433 0.1225 0.2505 -0.1159 0.1741  -0.0665 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.3528 0.1594 0.2322 -0.1149 0.1402  -0.0594 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.3077 0.1001 0.2615 -0.0999 0.1687  -0.0613 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2727 0.1075 0.2394 -0.0812 0.1237  -0.0498 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2782 0.1160 0.1823 -0.0962 0.1062  -0.0489 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2997 0.1085 0.1722 -0.1150 0.1245  -0.0547 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2556 0.0976 0.2887 -0.0643 0.1217  -0.0431 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2509 0.1226 0.2770 -0.0514 0.0806  -0.0349 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2330 0.0798 0.3447 -0.0508 0.1244  -0.0327 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2454 0.1143 0.1359 -0.0895 0.0730  -0.0388 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2549 0.1342 0.1090 -0.1023 0.0515  -0.0286 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2297 0.1328 0.1103 -0.0842 0.0328  -0.0210 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2540 0.1556 0.1185 -0.0959 0.0265  -0.0154 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2698 0.1670 0.1101 -0.1063 0.0325  -0.0166 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2892 0.2041 0.1209 -0.1165 0.0071  0.0034  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.3009 0.1710 0.1042 -0.1301 0.0470  -0.0226 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1892 0.1082 0.1036 -0.0593 0.0234  -0.0201 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1761 0.1076 0.1062 -0.0444 0.0088  -0.0149 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1630 0.0934 0.1099 -0.0259 -0.0009 -0.0154 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1402 0.0639 0.0976 -0.0240 0.0010  -0.0179 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1692 0.0998 0.1148 -0.0157 -0.0114 -0.0120 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1808 0.0940 0.1201 -0.0066 -0.0227 -0.0123 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1780 0.0822 0.0924 0.0004  -0.0196 -0.0094 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1667 0.0818 0.0884 0.0024  -0.0127 -0.0045 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2015 0.1026 0.1585 -0.0058 -0.0356 -0.0122 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2203 0.1279 0.1813 -0.0041 -0.0333 -0.0125 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1973 0.0994 0.1967 -0.0102 -0.0345 -0.0103 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2300 0.1218 0.2048 -0.0032 -0.0498 -0.0105 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1947 0.0733 0.0810 0.0025  -0.0216 -0.0106 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2122 0.0665 0.0700 0.0082  -0.0064 -0.0098 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2294 0.0663 0.0804 0.0101  -0.0050 -0.0116 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2426 0.0652 0.0856 0.0044  -0.0243 -0.0149 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.2565 0.0684 0.0662 0.0044  -0.0066 -0.0131 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.2779 0.0527 0.0554 0.0089  0.0224  -0.0134 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.2620 0.0939 0.0837 0.0042  -0.0060 -0.0104 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2390 0.0794 0.1041 0.0175  0.0175  -0.0060 125 SER   A N   
922  C CA  . SER   A 119 ? 0.2583 0.0834 0.1236 0.0203  0.0238  -0.0071 125 SER   A CA  
923  C C   . SER   A 119 ? 0.3271 0.1125 0.1763 0.0267  0.0598  -0.0059 125 SER   A C   
924  O O   . SER   A 119 ? 0.3696 0.1136 0.1898 0.0253  0.0701  -0.0130 125 SER   A O   
925  C CB  . SER   A 119 ? 0.2346 0.1073 0.1527 0.0215  0.0175  0.0028  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2744 0.1353 0.1998 0.0256  0.0254  0.0036  125 SER   A OG  
927  N N   . THR   A 120 ? 0.3468 0.1421 0.2211 0.0332  0.0832  0.0045  126 THR   A N   
928  C CA  . THR   A 120 ? 0.3991 0.1529 0.2737 0.0412  0.1302  0.0086  126 THR   A CA  
929  C C   . THR   A 120 ? 0.4499 0.1840 0.3071 0.0425  0.1501  0.0095  126 THR   A C   
930  O O   . THR   A 120 ? 0.4234 0.1890 0.2828 0.0388  0.1249  0.0106  126 THR   A O   
931  C CB  . THR   A 120 ? 0.3851 0.1774 0.3498 0.0516  0.1489  0.0326  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.3622 0.2167 0.3886 0.0503  0.1288  0.0542  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.3919 0.1945 0.3714 0.0511  0.1373  0.0322  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.5121 0.1905 0.3542 0.0476  0.2006  0.0092  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.5563 0.2121 0.3875 0.0501  0.2273  0.0117  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.6109 0.1909 0.4253 0.0552  0.2964  0.0101  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.6251 0.1650 0.4310 0.0559  0.3248  0.0054  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.6513 0.2078 0.4625 0.0586  0.3279  0.0140  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.7310 0.2050 0.5265 0.0633  0.4059  0.0125  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.7230 0.2317 0.6221 0.0803  0.4397  0.0404  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.6568 0.2578 0.6635 0.0891  0.4057  0.0680  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.7826 0.2116 0.6460 0.0815  0.5062  0.0350  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.7490 0.1996 0.7196 0.0988  0.5496  0.0643  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.6786 0.2133 0.6961 0.1005  0.4949  0.0805  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.6332 0.2235 0.7777 0.1136  0.5036  0.1166  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.7295 0.2170 0.8509 0.1170  0.5843  0.0999  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.8475 0.2382 0.9339 0.1180  0.6603  0.0856  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.9586 0.2372 0.9347 0.1088  0.7200  0.0587  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.8190 0.2424 0.9907 0.1260  0.6619  0.1031  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.6681 0.2040 0.5862 0.0855  0.4432  0.0567  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.6029 0.2092 0.5535 0.0850  0.3950  0.0676  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.5080 0.2103 0.5260 0.0830  0.3296  0.0830  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.4844 0.2452 0.5425 0.0808  0.2942  0.0968  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.4726 0.1838 0.4911 0.0805  0.3138  0.0788  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.4015 0.1892 0.4670 0.0747  0.2567  0.0906  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.4135 0.1909 0.3928 0.0632  0.2187  0.0613  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.4790 0.1945 0.3869 0.0604  0.2368  0.0403  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.3509 0.1658 0.5146 0.0816  0.2700  0.1192  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.3530 0.1820 0.6345 0.0932  0.3085  0.1593  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.3381 0.1724 0.7106 0.1013  0.3350  0.1851  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.3295 0.2280 0.6742 0.0839  0.2622  0.1887  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.3401 0.1736 0.3311 0.0542  0.1680  0.0630  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.3172 0.1490 0.2548 0.0451  0.1348  0.0422  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.2559 0.1425 0.2455 0.0396  0.1057  0.0556  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2229 0.1519 0.2597 0.0336  0.0904  0.0753  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.3335 0.1584 0.2150 0.0364  0.1097  0.0255  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.3023 0.1736 0.2205 0.0331  0.0937  0.0369  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.3427 0.1670 0.1919 0.0277  0.0779  0.0109  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2442 0.1230 0.2200 0.0386  0.0985  0.0468  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.2111 0.1315 0.2246 0.0314  0.0738  0.0577  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2252 0.1491 0.1984 0.0221  0.0454  0.0386  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.2546 0.1451 0.1829 0.0240  0.0446  0.0202  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1869 0.1447 0.1750 0.0085  0.0225  0.0452  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1641 0.1206 0.1243 -0.0001 0.0061  0.0284  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1440 0.1164 0.1192 -0.0098 -0.0045 0.0347  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1237 0.1168 0.1232 -0.0214 -0.0120 0.0553  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1529 0.1178 0.1013 -0.0122 -0.0008 0.0256  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1691 0.1252 0.1084 -0.0054 0.0074  0.0239  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1880 0.1214 0.1017 0.0002  0.0075  0.0091  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1558 0.1265 0.1162 -0.0077 0.0114  0.0409  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1842 0.1059 0.0842 0.0044  0.0142  0.0086  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1651 0.1262 0.1174 -0.0009 0.0214  0.0390  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1766 0.1118 0.0941 0.0052  0.0239  0.0213  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1450 0.1055 0.1075 -0.0076 -0.0081 0.0205  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1473 0.1174 0.1180 -0.0170 -0.0153 0.0235  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1621 0.1313 0.1137 -0.0366 -0.0178 0.0187  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1639 0.1193 0.1062 -0.0351 -0.0118 0.0043  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1513 0.1060 0.1198 -0.0075 -0.0161 0.0110  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1811 0.1580 0.1257 -0.0583 -0.0258 0.0329  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.2173 0.1756 0.1234 -0.0845 -0.0225 0.0266  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2459 0.1832 0.1403 -0.0881 -0.0087 0.0108  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.2354 0.1798 0.1467 -0.0810 -0.0133 0.0139  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2599 0.2217 0.1498 -0.1149 -0.0416 0.0506  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3669 0.2937 0.1949 -0.1505 -0.0374 0.0443  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3684 0.2829 0.1825 -0.1487 -0.0234 0.0307  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.4010 0.3051 0.1881 -0.1826 -0.0453 0.0519  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.2581 0.1671 0.1299 -0.0989 0.0124  -0.0048 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.2817 0.1635 0.1508 -0.1041 0.0356  -0.0178 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.3452 0.1806 0.1533 -0.1402 0.0586  -0.0249 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3757 0.1769 0.1749 -0.1486 0.0881  -0.0362 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2534 0.1335 0.1718 -0.0807 0.0505  -0.0284 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2392 0.1479 0.1953 -0.0541 0.0256  -0.0220 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2429 0.1088 0.1622 -0.0833 0.0680  -0.0355 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.3620 0.1888 0.1249 -0.1642 0.0477  -0.0177 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.4170 0.1862 0.1033 -0.2054 0.0686  -0.0252 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.4930 0.2243 0.1192 -0.2401 0.0688  -0.0210 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.5564 0.2192 0.1110 -0.2740 0.1029  -0.0353 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.4146 0.1852 0.0668 -0.2261 0.0466  -0.0133 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.3842 0.1825 0.0839 -0.1965 0.0514  -0.0193 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3960 0.1964 0.0646 -0.2185 0.0279  -0.0046 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3964 0.2469 0.1053 -0.2085 -0.0131 0.0238  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.4146 0.2813 0.1261 -0.2211 -0.0400 0.0462  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.4436 0.2808 0.1089 -0.2460 -0.0356 0.0420  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.3583 0.2698 0.1274 -0.2070 -0.0676 0.0741  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.4874 0.2548 0.1374 -0.2347 0.0349  -0.0014 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.5428 0.2753 0.1367 -0.2693 0.0305  0.0060  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.5631 0.2735 0.1711 -0.2556 0.0684  -0.0132 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.6028 0.2711 0.1537 -0.2867 0.0751  -0.0116 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.5343 0.3141 0.1589 -0.2708 -0.0201 0.0394  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.5200 0.3585 0.2378 -0.2212 -0.0254 0.0410  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.4840 0.3462 0.2506 -0.1847 -0.0123 0.0273  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.5038 0.3599 0.2411 -0.2222 -0.0440 0.0573  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.5256 0.2641 0.2120 -0.2119 0.0882  -0.0265 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.5207 0.2444 0.2405 -0.1971 0.1197  -0.0383 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.5884 0.2418 0.2741 -0.2156 0.1794  -0.0589 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.5689 0.2249 0.3171 -0.1912 0.2076  -0.0682 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.4511 0.2283 0.2696 -0.1494 0.1091  -0.0374 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.4214 0.2554 0.2696 -0.1304 0.0620  -0.0207 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3801 0.2468 0.2994 -0.0928 0.0534  -0.0223 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.4369 0.2770 0.2698 -0.1423 0.0443  -0.0081 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.6679 0.2516 0.2515 -0.2629 0.1996  -0.0638 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.7435 0.2387 0.2716 -0.2895 0.2675  -0.0858 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.7497 0.2227 0.3477 -0.2661 0.3260  -0.0983 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.7832 0.2032 0.3928 -0.2683 0.3889  -0.1138 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.8341 0.2445 0.2152 -0.3541 0.2738  -0.0874 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.8737 0.2950 0.1831 -0.3888 0.2123  -0.0671 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.9811 0.3019 0.1349 -0.4620 0.2176  -0.0659 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.8761 0.3162 0.2042 -0.3787 0.2081  -0.0703 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.7107 0.2262 0.3678 -0.2422 0.3058  -0.0886 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.6836 0.1904 0.4241 -0.2178 0.3492  -0.0928 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.6526 0.2012 0.5217 -0.1757 0.3574  -0.0885 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.6454 0.1763 0.5957 -0.1599 0.4019  -0.0882 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.6393 0.1831 0.4035 -0.2062 0.3165  -0.0811 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.5647 0.1974 0.3778 -0.1779 0.2441  -0.0641 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.5660 0.2276 0.3278 -0.1917 0.1924  -0.0517 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.4927 0.1868 0.4152 -0.1346 0.2198  -0.0555 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.5149 0.2483 0.3479 -0.1567 0.1475  -0.0396 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.4747 0.2247 0.3947 -0.1242 0.1615  -0.0432 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.4625 0.1642 0.4865 -0.1074 0.2409  -0.0532 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.4396 0.2412 0.4331 -0.0907 0.1284  -0.0348 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.4290 0.1878 0.5286 -0.0768 0.1966  -0.0401 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.4212 0.2239 0.4949 -0.0700 0.1431  -0.0337 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.6337 0.2358 0.5280 -0.1589 0.3138  -0.0814 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.6038 0.2395 0.6105 -0.1261 0.3153  -0.0735 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.6755 0.2501 0.7085 -0.1345 0.3890  -0.0833 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.6344 0.2273 0.7832 -0.1096 0.4015  -0.0712 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.5648 0.2539 0.5692 -0.1141 0.2610  -0.0666 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.5326 0.2815 0.5404 -0.0980 0.1971  -0.0547 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.5277 0.3106 0.5145 -0.0930 0.1590  -0.0507 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.4930 0.2736 0.5968 -0.0693 0.1798  -0.0421 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.7857 0.2827 0.7115 -0.1729 0.4373  -0.1025 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.8637 0.2846 0.7927 -0.1872 0.5190  -0.1162 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.9536 0.2903 0.8783 -0.2030 0.6025  -0.1272 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.9946 0.2612 0.9317 -0.2134 0.6809  -0.1384 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.9594 0.3282 0.7520 -0.2276 0.5256  -0.1328 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.9832 0.4158 0.7932 -0.2128 0.4699  -0.1243 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.9387 0.4217 0.8678 -0.1770 0.4618  -0.1121 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 1.0549 0.4855 0.7616 -0.2392 0.4322  -0.1267 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.9897 0.3207 0.8832 -0.2097 0.5939  -0.1263 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 1.0623 0.3027 0.9382 -0.2283 0.6790  -0.1382 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 1.0341 0.3152 1.0374 -0.1944 0.6787  -0.1207 145 GLU   A C   
1072 O O   . GLU   A 139 ? 1.0788 0.2907 1.0809 -0.2057 0.7484  -0.1278 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 1.1914 0.3521 0.8794 -0.2833 0.6864  -0.1562 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.2651 0.4932 0.9093 -0.2845 0.5960  -0.1426 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.4218 0.6156 0.8994 -0.3357 0.5560  -0.1467 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.4465 0.6685 0.8772 -0.3479 0.5000  -0.1343 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.4944 0.6328 0.8940 -0.3653 0.5786  -0.1589 145 GLU   A OE2 
1078 N N1  . A1BRE B .   ? 0.6767 0.1761 0.3537 0.0202  0.2179  -0.0386 201 A1BRE A N1  
1079 C C4  . A1BRE B .   ? 0.8055 0.1748 0.3112 -0.0025 0.2677  -0.0531 201 A1BRE A C4  
1080 C C5  . A1BRE B .   ? 0.7631 0.1993 0.3152 0.0001  0.2162  -0.0484 201 A1BRE A C5  
1081 C C6  . A1BRE B .   ? 0.6774 0.1865 0.3506 0.0212  0.2185  -0.0353 201 A1BRE A C6  
1082 C C7  . A1BRE B .   ? 0.7306 0.1612 0.3086 -0.0027 0.1962  -0.0564 201 A1BRE A C7  
1083 C C8  . A1BRE B .   ? 0.6916 0.1806 0.2870 -0.0086 0.1268  -0.0528 201 A1BRE A C8  
1084 C C10 . A1BRE B .   ? 0.5571 0.1981 0.3434 0.0291  0.1375  -0.0221 201 A1BRE A C10 
1085 C C13 . A1BRE B .   ? 0.7163 0.2306 0.3117 0.0023  0.1617  -0.0405 201 A1BRE A C13 
1086 O O1  . A1BRE B .   ? 0.4778 0.1940 0.3914 0.0463  0.1439  0.0015  201 A1BRE A O1  
1087 C C11 . A1BRE B .   ? 0.4877 0.2052 0.3652 0.0397  0.1230  -0.0052 201 A1BRE A C11 
1088 N N2  . A1BRE B .   ? 0.4370 0.2144 0.3460 0.0383  0.0885  0.0019  201 A1BRE A N2  
1089 C C9  . A1BRE B .   ? 0.6117 0.1946 0.3167 0.0112  0.1146  -0.0386 201 A1BRE A C9  
1090 C C12 . A1BRE B .   ? 0.6004 0.1868 0.3831 0.0358  0.2010  -0.0209 201 A1BRE A C12 
1091 O O   . A1BRE B .   ? 0.6165 0.1942 0.3749 0.0362  0.2188  -0.0175 201 A1BRE A O   
1092 N N   . A1BRE B .   ? 0.7552 0.1853 0.3207 0.0015  0.2209  -0.0507 201 A1BRE A N   
1093 C C3  . A1BRE B .   ? 0.7993 0.1898 0.3082 -0.0010 0.2590  -0.0482 201 A1BRE A C3  
1094 C C2  . A1BRE B .   ? 0.7416 0.2154 0.2970 0.0019  0.2009  -0.0398 201 A1BRE A C2  
1095 C C1  . A1BRE B .   ? 0.7005 0.2329 0.2975 0.0029  0.1546  -0.0366 201 A1BRE A C1  
1096 C C   . A1BRE B .   ? 0.6522 0.2593 0.2949 0.0040  0.1044  -0.0295 201 A1BRE A C   
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